PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9218959-1 1997 Elongation factor Tu (EF-Tu) is a G-protein which, in its active GTP conformation, protects and carries aminoacylated tRNAs (aa-tRNAs) to the ribosome during protein biosynthesis. Guanosine Triphosphate 65-68 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 9218959-1 1997 Elongation factor Tu (EF-Tu) is a G-protein which, in its active GTP conformation, protects and carries aminoacylated tRNAs (aa-tRNAs) to the ribosome during protein biosynthesis. Guanosine Triphosphate 65-68 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Triphosphate 180-183 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 55-60 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Triphosphate 180-183 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Triphosphate 180-183 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 9218959-4 1997 In its active form, EF-Tu.GTP without much further structural change interacts with aa-tRNAs in the so-called ternary complex. Guanosine Triphosphate 26-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 20-25 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 37-40 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 54-59 8665868-2 1996 Enacyloxin IIa [IC50 on poly(Phe) synthesis approximately 70 nM] is shown to affect the interaction between elongation factor (EF) Tu and GTP or GDP; in particular, the dissociation of EF-Tu-GTP is strongly retarded, causing the Kd of EF- Tu-GTP to decrease from 500 to 0.7 nM. Guanosine Triphosphate 138-141 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-133 8665868-3 1996 In its presence, the migration velocity of both GTP- and GDP-bound EF-Tu on native PAGE is increased. Guanosine Triphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 67-72 8557669-0 1996 Initial binding of the elongation factor Tu.GTP.aminoacyl-tRNA complex preceding codon recognition on the ribosome. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 23-43 8557669-1 1996 The first step in the sequence of interactions between the ribosome and the complex of elongation factor Tu (EF-Tu), GTP, and aminoacyl-tRNA, which eventually leads to A site-bound aminoacyl-tRNA, is the codon-independent formation of an initial complex. Guanosine Triphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 87-107 8557669-1 1996 The first step in the sequence of interactions between the ribosome and the complex of elongation factor Tu (EF-Tu), GTP, and aminoacyl-tRNA, which eventually leads to A site-bound aminoacyl-tRNA, is the codon-independent formation of an initial complex. Guanosine Triphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 109-114 8557669-6 1996 Hence, the ribosome-induced GTP hydrolysis by EF-Tu is strongly affected by the presence of the tRNA. Guanosine Triphosphate 28-31 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 46-51 8557669-7 1996 This suggests that codon-anticodon recognition, which takes place after the formation of the initial binding complex, provides a specific signal that triggers fast GTP hydrolysis by EF-Tu on the ribosome. Guanosine Triphosphate 164-167 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 182-187 8722020-4 1995 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Triphosphate 110-113 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 8722020-4 1995 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Triphosphate 110-113 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 8722020-5 1995 The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Guanosine Triphosphate 173-176 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 68-73 8722020-8 1995 We have previously found that two GTPs are hydrolyzed per peptide bond on EF-Tu, the implication being that two molecules of EF-Tu may interact on the ribosome to catalyze the binding of a single aa-tRNA to the A-site. Guanosine Triphosphate 34-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 8722020-8 1995 We have previously found that two GTPs are hydrolyzed per peptide bond on EF-Tu, the implication being that two molecules of EF-Tu may interact on the ribosome to catalyze the binding of a single aa-tRNA to the A-site. Guanosine Triphosphate 34-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 125-130 8722020-9 1995 More recently we found that ribosomes programmed with mRNA constructs other than poly(U), including the sequence AUGUUUACG, invariably use two GTPs per peptide bond in EF-Tu function. Guanosine Triphosphate 143-147 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 168-173 8722040-0 1995 Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 37-40 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 37-40 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 54-59 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 60-63 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 60-63 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 54-59 8722040-2 1995 Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu.GTP-aa-tRNA (ternary) and (EF-Tu.GTP)2.aa-tRNA (quinternary), can be formed in vitro depending on the conditions. Guanosine Triphosphate 60-63 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 54-59 8722040-8 1995 This, together with the results of time-resolved fluorescence measurements, suggests that codon recognition by the ternary complex on the ribosome initiates a series of structural rearrangements that result in a conformational change of EF-Tu, presumably involving the effector region, which, in turn, triggers GTP hydrolysis and the subsequent steps of A site binding. Guanosine Triphosphate 311-314 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 237-242 7794902-0 1995 Macromolecular arrangement in the aminoacyl-tRNA.elongation factor Tu.GTP ternary complex. Guanosine Triphosphate 70-73 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 49-69 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 33-38 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 163-166 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 33-38 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 163-166 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 7794902-5 1995 Formation of the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex was verified both by EF-Tu protection of the aminoacyl bond from chemical hydrolysis and by an EF-Tu.GTP-dependent increase in fluorescein intensity. Guanosine Triphosphate 163-166 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 7794902-6 1995 Spectral analyses revealed that both the emission intensity and lifetime of fluorescein were greater in the Phe-tRNAPhe-Fl8.EF-Tu.GTP ternary complex than in the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex. Guanosine Triphosphate 130-133 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 124-129 7794902-6 1995 Spectral analyses revealed that both the emission intensity and lifetime of fluorescein were greater in the Phe-tRNAPhe-Fl8.EF-Tu.GTP ternary complex than in the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex. Guanosine Triphosphate 130-133 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 178-183 7794902-6 1995 Spectral analyses revealed that both the emission intensity and lifetime of fluorescein were greater in the Phe-tRNAPhe-Fl8.EF-Tu.GTP ternary complex than in the Phe-tRNAPhe-Fl8.EF-Tu.GTP-Rh ternary complex. Guanosine Triphosphate 184-187 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 124-129 7782317-1 1995 The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. Guanosine Triphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 4-24 7782317-1 1995 The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. Guanosine Triphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 7782317-2 1995 After GTP hydrolysis EF-Tu is released in its GDP-bound state. Guanosine Triphosphate 6-9 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 21-26 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 82-102 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 104-109 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 133-138 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 139-142 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 82-102 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 139-142 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 104-109 7794902-2 1995 The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. Guanosine Triphosphate 139-142 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 133-138 7827027-2 1995 Two guanosine triphosphates (GTPs) are hydrolyzed on EF-Tu for every bound aa-tRNA. Guanosine Triphosphate 4-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 7827027-2 1995 Two guanosine triphosphates (GTPs) are hydrolyzed on EF-Tu for every bound aa-tRNA. Guanosine Triphosphate 29-33 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 7827027-3 1995 This was rationalized by the notion of an extended ternary complex, consisting of two EF-Tu.GTPs bound to a single aa-tRNA. Guanosine Triphosphate 92-96 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 86-91 7827027-4 1995 In this work, we combine fast kinetics with RNase A protection experiments to measure the stoichiometry between EF-Tu.GTP and aa-tRNA at 37 degrees C, where the binding is weak. Guanosine Triphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 112-117 7827027-5 1995 We find a 2:1 stoichiometry between EF-Tu.GTP and aa-tRNA at 37 degrees C, but at 0 degree C, under otherwise similar conditions, the stoichiometry of the complex is close to 1:1. Guanosine Triphosphate 42-45 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 36-41 7827027-7 1995 At 37 degrees C, aa-tRNA enters the A-site in a pentameric complex with two EF-Tu"s on which two GTPs are hydrolyzed in synchrony, when cognate codon-anticodon contact is established. Guanosine Triphosphate 97-101 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 76-81 7827027-8 1995 This pentameric model also explains how two GTPs can be hydrolyzed on EF-Tu, without rejection of 50% of the cognate aa-tRNAs in proofreading. Guanosine Triphosphate 44-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 70-75 7827027-10 1995 When the two EF-Tu bound GTPs are hydrolyzed, one aa-tRNA enters the A-site, and the other dissociates to the free state. Guanosine Triphosphate 25-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 13-18 7989307-7 1994 Thus, in eukaryotic protein synthesis, movement of transfer RNAs to the ribosome seems under the influence of two distinct molecules of EF-1 alpha, a result possibly related to the presumed consumption of two molecules of GTP by EF-Tu during the elongation step of prokaryotic protein synthesis. Guanosine Triphosphate 222-225 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 229-234 8433994-1 1993 Translation of the genetic code requires the accurate selection of elongation factor (EF)-Tu.GTP.tRNA ternary complexes at the ribosomal acceptor site, or A site. Guanosine Triphosphate 93-96 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 67-92 8048158-1 1994 In the elongation cycle of bacterial protein biosynthesis, the binding of aminoacyl-tRNA (aa-tRNA) to the A-site of mRNA-programmed ribosomes is mediated by elongation factor Tu (EF-Tu) and associated with the hydrolysis of GTP. Guanosine Triphosphate 224-227 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 157-177 8048158-1 1994 In the elongation cycle of bacterial protein biosynthesis, the binding of aminoacyl-tRNA (aa-tRNA) to the A-site of mRNA-programmed ribosomes is mediated by elongation factor Tu (EF-Tu) and associated with the hydrolysis of GTP. Guanosine Triphosphate 224-227 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 179-184 8375504-1 1993 This work studies the structure-function relationships of Asn135, a residue situated in the GTP binding pocket of elongation factor Tu (EF-Tu). Guanosine Triphosphate 92-95 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-134 8375504-1 1993 This work studies the structure-function relationships of Asn135, a residue situated in the GTP binding pocket of elongation factor Tu (EF-Tu). Guanosine Triphosphate 92-95 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 136-141 8075071-1 1994 Substitution Asp138-->Asn changes the substrate specificity of elongation factor (EF) Tu from GTP to XTP [Hwang & Miller (1987) J. Biol. Guanosine Triphosphate 97-100 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 66-91 8075071-6 1994 In poly(U)-directed poly(phenylalanine) synthesis, the number of peptide chains synthesized using EF-Tu D138N.XTP was 30% higher than with EF-Tu wild type (wt).GTP. Guanosine Triphosphate 160-163 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 108-130 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 79-99 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 108-130 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 101-106 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 79-99 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 101-106 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 248-251 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 79-99 8446899-1 1993 In the elongation cycle of bacterial protein synthesis the interaction between elongation factor-Tu (EF-Tu).guanosine triphosphate (GTP), aminoacyl-transfer RNA (aa-tRNA), and messenger RNA-programmed ribosomes is associated with the hydrolysis of GTP. Guanosine Triphosphate 248-251 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 101-106 8446899-3 1993 In the canonical scheme, one molecule of GTP is hydrolyzed in the EF-Tu-dependent binding of aa-tRNA to the ribosome, and a second molecule is hydrolyzed in the elongation factor-G (EF-G)-mediated translocation of the polypeptide from the ribosomal A site to the P site. Guanosine Triphosphate 41-44 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 66-71 8446899-4 1993 Substitution of Asp138 with Asn in EF-Tu changed the substrate specificity from GTP to xanthosine triphosphate and demonstrated that the EF-Tu-mediated reactions involved the hydrolysis of two nucleotide triphosphates for each Phe incorporated. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 35-40 8446899-4 1993 Substitution of Asp138 with Asn in EF-Tu changed the substrate specificity from GTP to xanthosine triphosphate and demonstrated that the EF-Tu-mediated reactions involved the hydrolysis of two nucleotide triphosphates for each Phe incorporated. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 137-142 2119812-1 1990 Mutagenesis was carried out in the N-terminal domain of elongation factor Tu (EF-Tu) to characterize the structure-function relationships of this model GTP binding protein with respect to stability, the interaction with GTP and GDP, and the catalytic activity. Guanosine Triphosphate 152-155 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 56-76 1899388-1 1991 This article reports on a comparison of the interaction of Al3+ and F- with two GTP-binding proteins, elongation factor Tu (EF-Tu) and the hormone sensitive regulatory protein (G protein) G0 alpha. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 102-122 1899388-1 1991 This article reports on a comparison of the interaction of Al3+ and F- with two GTP-binding proteins, elongation factor Tu (EF-Tu) and the hormone sensitive regulatory protein (G protein) G0 alpha. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 124-129 2119812-1 1990 Mutagenesis was carried out in the N-terminal domain of elongation factor Tu (EF-Tu) to characterize the structure-function relationships of this model GTP binding protein with respect to stability, the interaction with GTP and GDP, and the catalytic activity. Guanosine Triphosphate 152-155 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 78-83 2119812-1 1990 Mutagenesis was carried out in the N-terminal domain of elongation factor Tu (EF-Tu) to characterize the structure-function relationships of this model GTP binding protein with respect to stability, the interaction with GTP and GDP, and the catalytic activity. Guanosine Triphosphate 220-223 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 56-76 2190631-0 1990 Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Guanosine Triphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 86-106 2190631-0 1990 Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Guanosine Triphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 151-171 2190631-1 1990 The ubiquity of elongation factor Tu (EF-Tu)-dependent conformational changes in amino-acyl-tRNA (aa-tRNA) and the origin of the binding energy associated with aa-tRNA.EF-Tu.GTP ternary complex formation have been examined spectroscopically. Guanosine Triphosphate 174-177 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 16-36 2190631-1 1990 The ubiquity of elongation factor Tu (EF-Tu)-dependent conformational changes in amino-acyl-tRNA (aa-tRNA) and the origin of the binding energy associated with aa-tRNA.EF-Tu.GTP ternary complex formation have been examined spectroscopically. Guanosine Triphosphate 174-177 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 38-43 2190631-1 1990 The ubiquity of elongation factor Tu (EF-Tu)-dependent conformational changes in amino-acyl-tRNA (aa-tRNA) and the origin of the binding energy associated with aa-tRNA.EF-Tu.GTP ternary complex formation have been examined spectroscopically. Guanosine Triphosphate 174-177 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 168-173 2190631-4 1990 Upon association with EF-Tu.GTP, the emission intensities increased by 244%, 57%, or 15% for three aa-tRNAs due to a change in tRNA conformation; the fourth aa-tRNA exhibited no fluorescence change upon binding to EF-Tu.GTP. Guanosine Triphosphate 28-31 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 2190631-4 1990 Upon association with EF-Tu.GTP, the emission intensities increased by 244%, 57%, or 15% for three aa-tRNAs due to a change in tRNA conformation; the fourth aa-tRNA exhibited no fluorescence change upon binding to EF-Tu.GTP. Guanosine Triphosphate 28-31 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 214-219 2190631-4 1990 Upon association with EF-Tu.GTP, the emission intensities increased by 244%, 57%, or 15% for three aa-tRNAs due to a change in tRNA conformation; the fourth aa-tRNA exhibited no fluorescence change upon binding to EF-Tu.GTP. Guanosine Triphosphate 220-223 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 2190631-6 1990 Thus, the binding of EF-Tu.GTP induced or selected a tRNA conformation near s4U-8 that was very similar, and possibly the same, for each aa-tRNA species. Guanosine Triphosphate 27-30 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 21-26 2190631-9 1990 The Kd of the tRNA(Phe).EF-Tu.GTP ternary complex was determined, at equilibrium, to be 2.6 microM by the ability of the unacylated tRNA to compete with fluorescent Phe-tRNA for binding to the protein. Guanosine Triphosphate 30-33 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 24-29 2157708-0 1990 Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 102-122 2157708-8 1990 These results are in agreement with the observations derived from x-ray diffraction analysis that the tertiary structure of the GTP-binding domain of elongation factor Tu and that of p21 are similar. Guanosine Triphosphate 128-131 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 150-170 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Triphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 9-29 2110000-5 1990 The Kd for the Phe-tRNA(Phe)-Fl8.EF-Tu.GDP complex was found to average 28.5 microM, more than 33,000-fold greater than the Kd of the Phe-tRNA(Phe)-Fl8.EF-Tu.GTP complex under the same conditions. Guanosine Triphosphate 158-161 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 33-38 2110000-5 1990 The Kd for the Phe-tRNA(Phe)-Fl8.EF-Tu.GDP complex was found to average 28.5 microM, more than 33,000-fold greater than the Kd of the Phe-tRNA(Phe)-Fl8.EF-Tu.GTP complex under the same conditions. Guanosine Triphosphate 158-161 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 2110000-7 1990 Thus, the hydrolysis of the ternary complex GTP results in a dramatic decrease in the affinity of EF-Tu for aa-tRNA, thereby facilitating the release of EF-Tu.GDP from the aa-tRNA on the ribosome. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 2110000-7 1990 Thus, the hydrolysis of the ternary complex GTP results in a dramatic decrease in the affinity of EF-Tu for aa-tRNA, thereby facilitating the release of EF-Tu.GDP from the aa-tRNA on the ribosome. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 153-158 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Triphosphate 126-129 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Triphosphate 126-129 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 34203525-2 2021 Often described in the scientific literature under the collective name eEF1A, which stands for eukaryotic elongation factor 1A, their best known activity (in a monomeric, GTP-bound conformation) is to bind aminoacyl-tRNAs and deliver them to the A-site of the 80S ribosome. Guanosine Triphosphate 171-174 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 71-76 3170578-5 1988 The sequence of the GTP-binding site is consistent with predictions from other GTP-binding proteins such as elongation factor Tu or ras p21. Guanosine Triphosphate 20-23 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-128 3170578-5 1988 The sequence of the GTP-binding site is consistent with predictions from other GTP-binding proteins such as elongation factor Tu or ras p21. Guanosine Triphosphate 79-82 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-128 3181143-0 1988 Structure-function relationships in the GTP binding domain of EF-Tu: mutation of Val20, the residue homologous to position 12 in p21. Guanosine Triphosphate 40-43 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 62-67 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Triphosphate 126-129 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 2510820-9 1989 These results strongly support the hypothesis that aurodox not only confers a "GTP-like" conformation to the EF-Tu.GDP complex but also produces a less stable folding of the protein around the tryptophan residue that may contribute to the multiple functional effects of this antibiotic. Guanosine Triphosphate 79-82 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 109-114 2661226-16 1989 The rate of dissociation of the G domain complexes with GTP and GDP as well as the GTPase activity are also influenced by EF-Ts and kirromycin, but the effects evoked are small and in most cases different from those exerted on EF-Tu. Guanosine Triphosphate 56-59 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 227-232 2539860-1 1989 Different sites of the tRNA molecule influence the activity of the elongation factor Tu (EF-Tu) center for GTP hydrolysis [Parlato, G., Pizzano, R., Picone, D., Guesnet, J., Fasano, O., & Parmeggiani, A. Guanosine Triphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 67-87 2539860-1 1989 Different sites of the tRNA molecule influence the activity of the elongation factor Tu (EF-Tu) center for GTP hydrolysis [Parlato, G., Pizzano, R., Picone, D., Guesnet, J., Fasano, O., & Parmeggiani, A. Guanosine Triphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 89-94 2539860-10 1989 When EF-Tu acts as a component of the ternary complex formed with GTP and aa-tRNA, the presence of tRNA in the P-site strongly increases the GTPase activity. Guanosine Triphosphate 66-69 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 5-10 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Triphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Triphosphate 209-212 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 9-29 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Triphosphate 209-212 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 3181143-7 1988 As in p21, this position in EF-Tu is critical, influencing specifically the GDP/GTP interaction as well as other functions. Guanosine Triphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-33 3181143-9 1988 The differences observed with two homologous residues, Gly20 and Gly12 in EF-Tu and p21 respectively, show the importance of a variable residue in a consensus element in defining specific functions of GTP binding proteins. Guanosine Triphosphate 201-204 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 3104318-16 1987 Neither of these GTP gamma S-sensitive cysteines are in those regions of alpha 39 which are highly homologous to the GTP-binding site of elongation factor Tu (Jurnak, F. (1985) Science 230, 32-36). Guanosine Triphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 137-157 3554231-5 1987 Its GTPase shows the characteristics of a slow turnover reaction (0.1 mmol X sec-1 X mol-1 of G domain), whose rate closely corresponds to the initial hydrolysis rate of EF-Tu X GTP in the absence of effectors and lies in the typical range of GTPase of the p21 protein. Guanosine Triphosphate 4-7 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 170-175 3297141-5 1987 Compared with wild-type EF-Tu, EF-TuBo displays essentially the same affinity for GDP and GTP, with only the dissociation rate of EF-Tu GTP being slightly faster. Guanosine Triphosphate 90-93 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 3297141-6 1987 Protection of amino-acyl-tRNA (aa-tRNA) against nonenzymatic deacylation by different EF-Tu species indicates that conformational alterations occur in the ternary complex EF-TuBo GTP aa-tRNA. Guanosine Triphosphate 179-182 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 86-91 3302946-2 1987 Trans-diamminedichloroplatinum (II) was used to induce reversible crosslinks between EF-Tu and Phe-tRNA(Phe) within the ternary EF-Tu/GTP/Phe-tRNA(Phe) complex. Guanosine Triphosphate 134-137 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 3297780-2 1987 The conformation and topology as well as the affinity of the macromolecules in this ternary aa-tRNA X EF-Tu X GTP complex are of fundamental importance for the nature of the interaction of the complex with the ribosome. Guanosine Triphosphate 110-113 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 102-107 6609071-0 1984 Homologies in the primary structure of GTP-binding proteins: the nucleotide-binding site of EF-Tu and p21. Guanosine Triphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 92-97 3846595-1 1985 The exchange of elongation factor Tu (EF-Tu)-bound GTP in the presence and absence of elongation factor Ts (EF-Ts) was monitored by equilibrium exchange kinetic procedures. Guanosine Triphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 16-36 3846595-1 1985 The exchange of elongation factor Tu (EF-Tu)-bound GTP in the presence and absence of elongation factor Ts (EF-Ts) was monitored by equilibrium exchange kinetic procedures. Guanosine Triphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 38-43 3846595-2 1985 The kinetics of the exchange reaction were found to be consistent with the formation of a ternary complex EF-Tu X GTP X EF-Ts. Guanosine Triphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 106-111 3846595-3 1985 The equilibrium association constants of EF-Ts to the EF-Tu X GTP complex and of GTP to EF-Tu X EF-Ts were calculated to be 7 X 10(7) and 2 X 10(6) M-1, respectively. Guanosine Triphosphate 62-65 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 54-59 3846595-3 1985 The equilibrium association constants of EF-Ts to the EF-Tu X GTP complex and of GTP to EF-Tu X EF-Ts were calculated to be 7 X 10(7) and 2 X 10(6) M-1, respectively. Guanosine Triphosphate 81-84 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 88-93 3846595-5 1985 This is 500 times larger than the GTP dissociation rate constant from the EF-Tu X GTP complex (2.5 X 10(-2) s-1). Guanosine Triphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 3846595-5 1985 This is 500 times larger than the GTP dissociation rate constant from the EF-Tu X GTP complex (2.5 X 10(-2) s-1). Guanosine Triphosphate 82-85 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 3846595-6 1985 A procedure based on the observation that EF-Tu X GTP protects the aminoacyl-tRNA molecule from phosphodiesterase I-catalyzed hydrolysis was used to study the interactions of EF-Tu X GTP with Val-tRNAVal and Phe-tRNAPhe. Guanosine Triphosphate 50-53 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 3846595-6 1985 A procedure based on the observation that EF-Tu X GTP protects the aminoacyl-tRNA molecule from phosphodiesterase I-catalyzed hydrolysis was used to study the interactions of EF-Tu X GTP with Val-tRNAVal and Phe-tRNAPhe. Guanosine Triphosphate 50-53 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 175-180 3846595-7 1985 Binding constants of Phe-tRNAPhe and Val-tRNAVal to EF-Tu X GTP of 4.8 X 10(7) and 1.2 X 10(7)M-1, respectively, were obtained. Guanosine Triphosphate 60-63 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-57 3514605-0 1986 The reaction of ribosomes with elongation factor Tu.GTP complexes. Guanosine Triphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-51 3514605-3 1986 By measuring the rate constants for the reaction of poly(U)-programmed ribosomes with a binary complex of elongation factor (EF-Tu) and GTP we have shown that two of the key rate constants in the former reaction are determined exclusively by ribosome-EF-Tu interactions and are not affected by the aa-tRNA. Guanosine Triphosphate 136-139 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 125-130 3514605-3 1986 By measuring the rate constants for the reaction of poly(U)-programmed ribosomes with a binary complex of elongation factor (EF-Tu) and GTP we have shown that two of the key rate constants in the former reaction are determined exclusively by ribosome-EF-Tu interactions and are not affected by the aa-tRNA. Guanosine Triphosphate 136-139 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 251-256 3514605-4 1986 These are the rate constant for GTP hydrolysis, which plays an important role in the fidelity of ternary complex selection by the ribosome, and the rate constant for EF-Tu.GDP dissociation from the ribosome, which plays an equally important role in subsequent proofreading of the aa-tRNA. Guanosine Triphosphate 32-35 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 166-171 3514605-6 1986 These interactions determine the absolute value of the rate constants for GTP hydrolysis and EF-Tu.GDP dissociation. Guanosine Triphosphate 74-77 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 93-98 6377304-4 1984 In the case of elongation factor Tu X GDP X kirromycin, cross-linking was found at lysine-208; in elongation factor Tu X GTP X kirromycin, cross-linking was at lysine-208 and lysine-237. Guanosine Triphosphate 121-124 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-118 6112013-0 1981 Altered regulation of the guanosine 5"-triphosphate activity in a kirromycin-resistant elongation factor Tu. Guanosine Triphosphate 26-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 87-107 7040360-0 1982 Interaction of aminoacyl-tRNA with bacterial elongation factor Tu: GTP complex: effects of the amino group of amino acid esterified to tRNA, the amino acid side chain, and tRNA structure. Guanosine Triphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 45-65 7040360-3 1982 The results indicated that the free amino-acid group of the amino acids in aminoacyl-tRNA is strongly required for binding with EF-Tu : GTP. Guanosine Triphosphate 136-139 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 128-133 6323160-5 1984 The Ala-375 replacements also lower the dissociation rates of the binary complexes EF-Tu.GTP and the binding constants for EF-Tu.GTP and Phe-tRNA. Guanosine Triphosphate 89-92 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 6323160-5 1984 The Ala-375 replacements also lower the dissociation rates of the binary complexes EF-Tu.GTP and the binding constants for EF-Tu.GTP and Phe-tRNA. Guanosine Triphosphate 129-132 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-88 6323160-5 1984 The Ala-375 replacements also lower the dissociation rates of the binary complexes EF-Tu.GTP and the binding constants for EF-Tu.GTP and Phe-tRNA. Guanosine Triphosphate 129-132 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 123-128 6323160-10 1984 It increases the dissociation rate of EF-Tu.GTP by approximately 30%. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 38-43 6130090-5 1983 In the absence of ribosomes and at low [Mg2+], the one-round GTP hydrolysis by EF-Tu is enhanced by C-C-A-aa fragments, whereas it is inhibited by the corresponding aa-tRNAs. Guanosine Triphosphate 61-64 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 79-84 7041970-0 1982 Elongation factor Tu.ribosome dependent guanosine 5"-triphosphate hydrolysis: elucidation of the role of the aminoacyl transfer ribonucleic acid 3" terminus and site(s) involved in the inducing of the guanosinetriphosphatase reaction. Guanosine Triphosphate 40-65 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 6765192-8 1982 Moreover, NEM modification also indicates an additional tRNA binding site on EF-Tu.GTP.kirromycin, which could not be detected with TPCK. Guanosine Triphosphate 83-86 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 77-82 6114863-0 1981 Effects of antibiotics, N-acetylaminoacyl-tRNA and other agents on the elongation-factor-Tu dependent and ribosome-dependent GTP hydrolysis promoted by 2"(3")-O-L-phenylalanyladenosine. Guanosine Triphosphate 125-128 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 71-91 6112013-4 1981 As additional effect, the mutation caused an increased affinity of EF-Tu for GTP. Guanosine Triphosphate 77-80 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 67-72 6112013-5 1981 Ammonium dependence of the GTPase activity an increased affinity for GTP are two properties also found with wild-type EF-Tu in the presence of kirromycin [Fasano, O., Burns, W., Crechet, J.-B., Sander, G., & Parmeggiani, A. Guanosine Triphosphate 27-30 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 118-123 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Triphosphate 127-130 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-72 371979-0 1979 Hydrolysis of GTP by the elongation factor Tu.kirromycin complex. Guanosine Triphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 25-45 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 266-269 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 129-149 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 266-269 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 151-156 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 266-269 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 266-269 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 266-269 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 324-327 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 129-149 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 324-327 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 151-156 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 324-327 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 324-327 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Triphosphate 324-327 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-2 1978 Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin. Guanosine Triphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 21-26 364475-3 1978 As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Guanosine Triphosphate 164-167 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 158-163 364475-3 1978 As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Guanosine Triphosphate 164-167 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 212-217 356044-1 1978 Complex formation between elongation factor Tu, GTP, and Nepsilon-bromoacetyl-Lys-tRNA results in the cross-linking of the protein and the modified Lys-tRNA. Guanosine Triphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-46 350580-5 1978 GTP was determined by circular dichroism titrations to be 4 x 10(6) M-1, and to EF-Tu . Guanosine Triphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 80-85 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Triphosphate 127-130 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 187578-7 1976 The spectra of spin-labeled EF-Tu-GDP changed markedly when its GDP moiety was replaced by GTP through incubation with phosphoenolpyruvate and pyruvate kinase [EC 2.7.1.40], the broad component increasing at the expense of the narrow component. Guanosine Triphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-33 187578-9 1976 The GTP-induced spectral change was reversed upon conversion of labeled EF-Tu-GTP to EF-Tu-GDP by addition of excess GDP. Guanosine Triphosphate 4-7 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 187578-9 1976 The GTP-induced spectral change was reversed upon conversion of labeled EF-Tu-GTP to EF-Tu-GDP by addition of excess GDP. Guanosine Triphosphate 4-7 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 1099087-3 1975 The conformational difference between polypeptide chain elongation factor Tu (EF-Tu)-GTP and EF-Tu-GDP has been studied using hydrophobic and fluorescent probes. Guanosine Triphosphate 85-88 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 56-76 1099087-3 1975 The conformational difference between polypeptide chain elongation factor Tu (EF-Tu)-GTP and EF-Tu-GDP has been studied using hydrophobic and fluorescent probes. Guanosine Triphosphate 85-88 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 78-83 1099087-16 1975 249, 3311), demonstrate that reversible conformational transition does occur in EF-Tu on changing the ligand from GDP to GTP. Guanosine Triphosphate 121-124 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 80-85 1097432-2 1975 The role of guanosine triphosphate (GTP) in the elongation factor Tu(EF-Tu)promoted binding of aminoacyl-tRNA to ribosomes has been investigated. Guanosine Triphosphate 12-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 48-68 1097432-2 1975 The role of guanosine triphosphate (GTP) in the elongation factor Tu(EF-Tu)promoted binding of aminoacyl-tRNA to ribosomes has been investigated. Guanosine Triphosphate 12-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 1097432-2 1975 The role of guanosine triphosphate (GTP) in the elongation factor Tu(EF-Tu)promoted binding of aminoacyl-tRNA to ribosomes has been investigated. Guanosine Triphosphate 36-39 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 48-68 1097432-2 1975 The role of guanosine triphosphate (GTP) in the elongation factor Tu(EF-Tu)promoted binding of aminoacyl-tRNA to ribosomes has been investigated. Guanosine Triphosphate 36-39 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 1097432-7 1975 It was concluded that the role of GTP in this reaction is to facilitate the transfer of Phe-tRNA to ribosomes by virtue of the high affinity of EF-Tu.GTP for ribosomes. Guanosine Triphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 145-150 1097432-7 1975 It was concluded that the role of GTP in this reaction is to facilitate the transfer of Phe-tRNA to ribosomes by virtue of the high affinity of EF-Tu.GTP for ribosomes. Guanosine Triphosphate 151-154 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 145-150 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 1097432-9 1975 Thus, the hydrolysis of GTP seems to be required for the release of EF-Tu from ribosomes, which is necessary for peptidyl transfer and the reutilization of EF-Tu. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 68-73 1097432-9 1975 Thus, the hydrolysis of GTP seems to be required for the release of EF-Tu from ribosomes, which is necessary for peptidyl transfer and the reutilization of EF-Tu. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 156-161 4373734-3 1974 Formation of the EF-Tu.GTP complex is strongly stimulated. Guanosine Triphosphate 23-26 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 17-22 4373734-5 1974 This antibiotic also enables EF-Tu to catalyze the binding of Phe-tRNA(Phe) to the poly(U).ribosome complex even in the absence of GTP. Guanosine Triphosphate 131-134 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 4373734-6 1974 EF-Tu activity in the GTPase reaction is dramatically affected by kirromycin: GTP hydrolysis, which normally requires ribosomes and aminoacyl-tRNA, takes place with the elongation factor alone. Guanosine Triphosphate 22-25 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-5 4373734-10 1974 In conclusion, kirromycin can substitute for GTP, aminoacyl-tRNA, or ribosomes in various reactions involving EF-Tu, apparently by affecting the allosteric controls between the sites on the EF-Tu molecule interacting with these components. Guanosine Triphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 110-115 4373734-10 1974 In conclusion, kirromycin can substitute for GTP, aminoacyl-tRNA, or ribosomes in various reactions involving EF-Tu, apparently by affecting the allosteric controls between the sites on the EF-Tu molecule interacting with these components. Guanosine Triphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 190-195 4741543-0 1973 Evidence for conformational changes in elongation factor Tu induced by GTP and GDP. Guanosine Triphosphate 71-74 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 39-59 31058500-4 2019 EF-Tu alternates between GTP- and GDP-bound conformations during its functional cycle, representing the "on" and "off" states, respectively. Guanosine Triphosphate 25-28 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-5 32024753-6 2020 aa-tRNAs failing to undergo peptide bond formation at the end of accommodation corridor passage after EF-Tu release can be reengaged by EF-Tu GTP from solution, coupled to GTP hydrolysis. Guanosine Triphosphate 142-145 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 102-107 32024753-6 2020 aa-tRNAs failing to undergo peptide bond formation at the end of accommodation corridor passage after EF-Tu release can be reengaged by EF-Tu GTP from solution, coupled to GTP hydrolysis. Guanosine Triphosphate 142-145 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 136-141 32024753-6 2020 aa-tRNAs failing to undergo peptide bond formation at the end of accommodation corridor passage after EF-Tu release can be reengaged by EF-Tu GTP from solution, coupled to GTP hydrolysis. Guanosine Triphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 102-107 32024753-6 2020 aa-tRNAs failing to undergo peptide bond formation at the end of accommodation corridor passage after EF-Tu release can be reengaged by EF-Tu GTP from solution, coupled to GTP hydrolysis. Guanosine Triphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 136-141 31711607-0 2020 tRNA Dissociation from EF-Tu after GTP Hydrolysis: Primary Steps and Antibiotic Inhibition. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 23-28 31711607-2 2020 After successful decoding, EF-Tu hydrolyzes GTP, which triggers a conformational change that ultimately results in the release of the tRNA from EF-Tu. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-32 31711607-2 2020 After successful decoding, EF-Tu hydrolyzes GTP, which triggers a conformational change that ultimately results in the release of the tRNA from EF-Tu. Guanosine Triphosphate 44-47 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 144-149 31711607-4 2020 Our results suggest that after GTP hydrolysis and Pi release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. Guanosine Triphosphate 31-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 135-140 31711607-4 2020 Our results suggest that after GTP hydrolysis and Pi release, the loss of interactions between the nucleotide and the switch 1 loop of EF-Tu allows domain D1 of EF-Tu to rotate relative to domains D2 and D3 and leads to an increased flexibility of the switch 1 loop. Guanosine Triphosphate 31-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 161-166 31058500-6 2019 Additionally, molecular dynamics (MD) simulations indicate that enthalpic stabilization of GDP binding compared to GTP binding originates in the backbone hydrogen bonding network of EF-Tu. Guanosine Triphosphate 115-118 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 182-187 31058500-7 2019 In contrast, binding of GTP to EF-Tu is entropically driven by the liberation of bound water during the GDP- to GTP-bound transition. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 31058500-7 2019 In contrast, binding of GTP to EF-Tu is entropically driven by the liberation of bound water during the GDP- to GTP-bound transition. Guanosine Triphosphate 112-115 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 30108131-3 2018 Here, we demonstrate that GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner. Guanosine Triphosphate 26-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 43-48 30370994-4 2019 The remaining subunits of the eEF1 complex, eEF1Balpha, eEF1Bdelta, eEF1Bgamma, and valyl-tRNA synthetase (VARS), together form the GTP exchange factor for eEF1A and are ubiquitously expressed, in keeping with their housekeeping role. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 30-34 30370994-4 2019 The remaining subunits of the eEF1 complex, eEF1Balpha, eEF1Bdelta, eEF1Bgamma, and valyl-tRNA synthetase (VARS), together form the GTP exchange factor for eEF1A and are ubiquitously expressed, in keeping with their housekeeping role. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 156-161 29417736-4 2018 We hypothesize that the exit rate of eukaryotic translation elongation factor 1A (eEF1A)*GDP from the 80S ribosome depends on the protein affinity to specific aminoacyl-tRNA remaining on the ribosome after GTP hydrolysis. Guanosine Triphosphate 206-209 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 37-80 29792818-2 2018 We use recent experimental data to discuss how induced fit affects accuracy of initial codon selection on the ribosome by aminoacyl transfer RNA in ternary complex ( T3) with elongation factor Tu (EF-Tu) and guanosine-5"-triphosphate (GTP). Guanosine Triphosphate 235-238 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 175-195 29792818-2 2018 We use recent experimental data to discuss how induced fit affects accuracy of initial codon selection on the ribosome by aminoacyl transfer RNA in ternary complex ( T3) with elongation factor Tu (EF-Tu) and guanosine-5"-triphosphate (GTP). Guanosine Triphosphate 235-238 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 197-202 29417736-4 2018 We hypothesize that the exit rate of eukaryotic translation elongation factor 1A (eEF1A)*GDP from the 80S ribosome depends on the protein affinity to specific aminoacyl-tRNA remaining on the ribosome after GTP hydrolysis. Guanosine Triphosphate 206-209 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 82-87 29459784-4 2018 Our results suggest that 2"-O-methylation sterically perturbs interactions of ribosomal-monitoring bases (G530, A1492 and A1493) with cognate codon-anticodon helices, thereby inhibiting downstream GTP hydrolysis by elongation factor Tu (EF-Tu) and A-site tRNA accommodation, leading to excessive rejection of cognate aminoacylated tRNAs in initial selection and proofreading. Guanosine Triphosphate 197-200 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 215-235 29459784-4 2018 Our results suggest that 2"-O-methylation sterically perturbs interactions of ribosomal-monitoring bases (G530, A1492 and A1493) with cognate codon-anticodon helices, thereby inhibiting downstream GTP hydrolysis by elongation factor Tu (EF-Tu) and A-site tRNA accommodation, leading to excessive rejection of cognate aminoacylated tRNAs in initial selection and proofreading. Guanosine Triphosphate 197-200 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 237-242 28108655-3 2017 We here demonstrate, using a wide range of in vitro and in vivo approaches, that the previously uncharacterized human methyltransferase METTL21B specifically targets Lys-165 in eEF1A in an aminoacyl-tRNA- and GTP-dependent manner. Guanosine Triphosphate 209-212 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 177-182 29045140-2 2017 Upon binding to the ribosome, EF-Tu undergoes GTP hydrolysis, which drives a major conformational change, triggering the release of aminoacylated tRNA to the ribosome. Guanosine Triphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 30-35 29045140-4 2017 We show that the transition free energy is minimal along a non-intuitive pathway that involves "separation" of the GTP binding domain (domain 1) from the OB folds (domains 2 and 3), followed by domain 1 rotation, and, eventually, locking the EF-Tu conformation in the post-hydrolysis state. Guanosine Triphosphate 115-118 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 242-247 26651998-4 2015 Using a ternatin photo-affinity probe, we identify the translation elongation factor-1A ternary complex (eEF1A GTP aminoacyl-tRNA) as a specific target and demonstrate competitive binding by the unrelated natural products, didemnin and cytotrienin. Guanosine Triphosphate 111-114 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 105-110 26653849-0 2016 Theoretical Insights on the Mechanism of the GTP Hydrolysis Catalyzed by the Elongation Factor Tu (EF-Tu). Guanosine Triphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 77-97 26653849-0 2016 Theoretical Insights on the Mechanism of the GTP Hydrolysis Catalyzed by the Elongation Factor Tu (EF-Tu). Guanosine Triphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-104 26653849-1 2016 The purpose of this work is to have a better understanding of the mechanism of GTP hydrolysis catalyzed by the elongation factor Tu. Guanosine Triphosphate 79-82 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 111-131 26073967-8 2015 These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. Guanosine Triphosphate 131-134 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 118-123 24990941-0 2014 Direct evidence of an elongation factor-Tu/Ts GTP Aminoacyl-tRNA quaternary complex. Guanosine Triphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-42 26073967-4 2015 During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. Guanosine Triphosphate 26-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 20-25 26073967-5 2015 GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. Guanosine Triphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 70-75 25566871-4 2015 We have used rapid-kinetics measurements in vitro and molecular dynamics (MD) simulations in silico to investigate the relationship between GTP-binding properties and P-loop structural dynamics in the universally conserved Elongation Factor (EF) Tu. Guanosine Triphosphate 140-143 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 223-248 25566871-5 2015 Analysis of wild type EF-Tu and variants with substitutions at positions in or adjacent to the P-loop revealed a correlation between P-loop flexibility and the entropy of activation for GTP dissociation. Guanosine Triphosphate 186-189 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 25566871-6 2015 The same variants demonstrate more backbone flexibility in two N-terminal amino acids of the P-loop during force-induced EF-Tu GTP dissociation in Steered Molecular Dynamics simulations. Guanosine Triphosphate 129-132 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 121-126 25436608-1 2014 Translation elongation is the stage of protein synthesis in which the translation factor eEF1A plays a pivotal role that is dependent on GTP exchange. Guanosine Triphosphate 137-140 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 89-94 25436608-3 2014 The GTP exchange factor for eEF1A1 is a complex called eEF1B made up of subunits eEF1Balpha, eEF1Bdelta and eEF1Bgamma. Guanosine Triphosphate 4-7 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-34 25326326-1 2014 Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. Guanosine Triphosphate 56-59 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 25326326-2 2014 eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Guanosine Triphosphate 6-9 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-5 25326326-3 2014 Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. Guanosine Triphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 93-98 25326326-7 2014 Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. Guanosine Triphosphate 221-224 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 71-76 25326326-7 2014 Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. Guanosine Triphosphate 221-224 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 112-117 25225612-3 2014 Here, we provide biochemical and high-resolution structural evidence that eIF5B and aEF1A/EF-Tu bound to GTP or GTPgammaS coordinate a monovalent cation (M(+)) in their active site. Guanosine Triphosphate 105-108 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 90-95 25246550-1 2014 GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. Guanosine Triphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 18-38 25246550-1 2014 GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. Guanosine Triphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-45 25246550-3 2014 Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Guanosine Triphosphate 141-144 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 159-164 25246550-6 2014 In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K(+) ions. Guanosine Triphosphate 104-107 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 24990941-1 2014 During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. Guanosine Triphosphate 64-67 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-46 24990941-1 2014 During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. Guanosine Triphosphate 64-67 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 48-53 24990941-6 2014 A central feature of this model is the existence of a quaternary complex of EF-Tu/Ts GTP aa-tRNA(aa). Guanosine Triphosphate 85-88 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 76-81 24564225-4 2014 RESULTS: Through sequence searching of genomic and EST databases, we find a striking association of eEF1A replacement by EFL and loss of eEF1A"s guanine exchange factor, eEF1Balpha, suggesting that EFL is able to spontaneously recharge with GTP. Guanosine Triphosphate 241-244 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 100-105 24564225-4 2014 RESULTS: Through sequence searching of genomic and EST databases, we find a striking association of eEF1A replacement by EFL and loss of eEF1A"s guanine exchange factor, eEF1Balpha, suggesting that EFL is able to spontaneously recharge with GTP. Guanosine Triphosphate 241-244 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 137-142 22740700-2 2012 By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and release of Sec-tRNA(Sec) to the ribosome by the structural switch between GTP- and GDP-bound conformations. Guanosine Triphosphate 163-166 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 14-34 23864225-0 2013 Mechanism of activation of elongation factor Tu by ribosome: catalytic histidine activates GTP by protonation. Guanosine Triphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-47 23864225-2 2013 Release of EF-Tu, after correct binding of the EF-Tu:aa-tRNA complex to the ribosome, is initiated by GTP hydrolysis. Guanosine Triphosphate 102-105 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 11-16 23864225-2 2013 Release of EF-Tu, after correct binding of the EF-Tu:aa-tRNA complex to the ribosome, is initiated by GTP hydrolysis. Guanosine Triphosphate 102-105 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 47-52 23864225-4 2013 There have been a number of mechanistic proposals, including those spurred by a recent X-ray crystallographic analysis of a ribosome:EF-Tu:aa-tRNA:GTP-analog complex. Guanosine Triphosphate 147-150 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 133-138 23864225-8 2013 Given the similarity between EF-Tu and other members of the translational G-protein family, it is likely that these mechanisms of ribosome-activated GTP hydrolysis are pertinent to all of these proteins. Guanosine Triphosphate 149-152 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 22740700-2 2012 By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and release of Sec-tRNA(Sec) to the ribosome by the structural switch between GTP- and GDP-bound conformations. Guanosine Triphosphate 163-166 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 36-41 21719661-2 2011 (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. Guanosine Triphosphate 148-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 63-83 22459262-4 2012 Recent biochemical and structural studies indicate that the SRL is critical for triggering GTP hydrolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF-G). Guanosine Triphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 109-129 22459262-4 2012 Recent biochemical and structural studies indicate that the SRL is critical for triggering GTP hydrolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF-G). Guanosine Triphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 131-136 22437501-2 2012 tRNA selection is initiated by elongation factor Tu, which delivers tRNA to the aminoacyl tRNA-binding site (A site) and hydrolyses GTP upon establishing codon-anticodon interactions in the decoding centre. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-51 22378069-3 2012 Interestingly, S21 belongs to the first eEF1A GTP/GDP-binding consensus sequence. Guanosine Triphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-45 21665947-1 2011 Translation elongation in eukaryotes is mediated by the concerted actions of elongation factor 1A (eEF1A), which delivers aminoacylated tRNA to the ribosome; elongation factor 1B (eEF1B) complex, which catalyzes the exchange of GDP to GTP on eEF1A; and eEF2, which facilitates ribosomal translocation. Guanosine Triphosphate 235-238 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-104 21719661-2 2011 (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. Guanosine Triphosphate 148-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 21719661-2 2011 (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. Guanosine Triphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 63-83 21719661-2 2011 (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. Guanosine Triphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 21719661-3 2011 However, their identification of histidine-84 of EF-Tu as deprotonating the catalytic water molecule is problematic in relation to their atomic structure; the terminal phosphate of GTP is more likely to be the proper proton acceptor. Guanosine Triphosphate 181-184 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 49-54 17397188-1 2007 Elongation factor Tu (EF-Tu) belongs to the family of GTP-binding proteins and requires elongation factor Ts (EF-Ts) for nucleotide exchange. Guanosine Triphosphate 54-57 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 20838377-5 2011 Notably, eEF1A has GTPase activity and can exist in GTP- or GDP-bound forms, which are associated with distinct structural conformations of the protein. Guanosine Triphosphate 19-22 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 9-14 20838377-6 2011 Here, we show that the guanine nucleotide-bound state of eEF1A regulates its ability to activate SK1, with eEF1A.GDP, but not eEF1A.GTP, enhancing SK1 activity in vitro. Guanosine Triphosphate 132-135 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 57-62 17951333-2 2007 Allosteric coupling of GTP hydrolysis by elongation factor Tu (EF-Tu) at the ribosomal GTPase center to messenger RNA (mRNA) codon:aminoacyl-transfer RNA (aa-tRNA) anticodon recognition at the ribosomal decoding site is essential for accurate and rapid aa-tRNA selection. Guanosine Triphosphate 23-26 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 41-61 17951333-2 2007 Allosteric coupling of GTP hydrolysis by elongation factor Tu (EF-Tu) at the ribosomal GTPase center to messenger RNA (mRNA) codon:aminoacyl-transfer RNA (aa-tRNA) anticodon recognition at the ribosomal decoding site is essential for accurate and rapid aa-tRNA selection. Guanosine Triphosphate 23-26 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 63-68 17951333-3 2007 Here we use single-molecule methods to investigate the mechanism of action of the antibiotic thiostrepton and show that the GTPase center of the ribosome has at least two discrete functions during aa-tRNA selection: binding of EF-Tu(GTP) and stimulation of GTP hydrolysis by the factor. Guanosine Triphosphate 124-127 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 227-237 21051640-2 2010 To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. Guanosine Triphosphate 40-43 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 125-130 21051640-2 2010 To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. Guanosine Triphosphate 72-75 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 125-130 21051640-3 2010 EF-Tu is in its active conformation, the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. Guanosine Triphosphate 190-193 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-5 20434456-3 2010 The ribosome actively facilitates this process by recognizing structural features of the correct substrate, initiated in its decoding site, to accelerate the rates of elongation factor-Tu-catalyzed GTP hydrolysis and ribosome-catalyzed peptide bond formation. Guanosine Triphosphate 198-201 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 167-187 19833920-2 2009 Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. Guanosine Triphosphate 94-116 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 47-67 19833920-2 2009 Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. Guanosine Triphosphate 94-116 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 19833920-2 2009 Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. Guanosine Triphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 47-67 19833920-2 2009 Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. Guanosine Triphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 18773979-0 2008 Mechanism of the chemical step for the guanosine triphosphate (GTP) hydrolysis catalyzed by elongation factor Tu. Guanosine Triphosphate 39-61 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 92-112 18773979-0 2008 Mechanism of the chemical step for the guanosine triphosphate (GTP) hydrolysis catalyzed by elongation factor Tu. Guanosine Triphosphate 63-66 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 92-112 18773979-1 2008 Elongation factor Tu (EF-Tu), the protein responsible for delivering aminoacyl-tRNAs (aa-tRNAs) to ribosomal A site during translation, belongs to the group of guanosine-nucleotide (GTP/GDP) binding proteins. Guanosine Triphosphate 182-185 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 18773979-1 2008 Elongation factor Tu (EF-Tu), the protein responsible for delivering aminoacyl-tRNAs (aa-tRNAs) to ribosomal A site during translation, belongs to the group of guanosine-nucleotide (GTP/GDP) binding proteins. Guanosine Triphosphate 182-185 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 18773979-5 2008 In the first case we presumably mimic binding of the ternary complex EF-Tu.GTP.aa-tRNA to the ribosome and allow the histidine (His85) side chain of the protein to approach the reaction active site. Guanosine Triphosphate 75-78 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 18773979-6 2008 In the second case, corresponding to the GTP hydrolysis by EF-Tu alone, the side chain of His85 stays away from the active site, and the chemical reaction GTP+H(2)O-->GDP+Pi proceeds without participation of the histidine but through water molecules. Guanosine Triphosphate 41-44 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 59-64 18773979-6 2008 In the second case, corresponding to the GTP hydrolysis by EF-Tu alone, the side chain of His85 stays away from the active site, and the chemical reaction GTP+H(2)O-->GDP+Pi proceeds without participation of the histidine but through water molecules. Guanosine Triphosphate 155-158 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 59-64 18773979-7 2008 In agreement with the experimental observations which distinguish rate constants for the fast chemical reaction in EF-Tu.GTP.aa-tRNA.ribosome and the slow spontaneous GTP hydrolysis in EF-Tu, we show that the activation energy barrier for the first scenario is considerably lower compared to that of the second case. Guanosine Triphosphate 121-124 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 115-120 18773979-7 2008 In agreement with the experimental observations which distinguish rate constants for the fast chemical reaction in EF-Tu.GTP.aa-tRNA.ribosome and the slow spontaneous GTP hydrolysis in EF-Tu, we show that the activation energy barrier for the first scenario is considerably lower compared to that of the second case. Guanosine Triphosphate 121-124 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 185-190 18773979-7 2008 In agreement with the experimental observations which distinguish rate constants for the fast chemical reaction in EF-Tu.GTP.aa-tRNA.ribosome and the slow spontaneous GTP hydrolysis in EF-Tu, we show that the activation energy barrier for the first scenario is considerably lower compared to that of the second case. Guanosine Triphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 115-120 18773979-7 2008 In agreement with the experimental observations which distinguish rate constants for the fast chemical reaction in EF-Tu.GTP.aa-tRNA.ribosome and the slow spontaneous GTP hydrolysis in EF-Tu, we show that the activation energy barrier for the first scenario is considerably lower compared to that of the second case. Guanosine Triphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 185-190 18789156-8 2008 In a pull-down assay, elongation factor Tu (EF-Tu), a GTP-binding protein involved in protein translation, usually found in cytoplasm, was recovered among LVS bacterial membrane proteins bound on RGG domain of nucleolin. Guanosine Triphosphate 54-57 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-42 18789156-8 2008 In a pull-down assay, elongation factor Tu (EF-Tu), a GTP-binding protein involved in protein translation, usually found in cytoplasm, was recovered among LVS bacterial membrane proteins bound on RGG domain of nucleolin. Guanosine Triphosphate 54-57 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 44-49 18336835-2 2008 We use molecular dynamics simulations to investigate the dynamics of the EF-Tu.guanosine 5"-triphosphate.aa-tRNA(Cys) complex and the roles played by Mg2+ ions and modified nucleosides on the free energy of protein.RNA binding. Guanosine Triphosphate 79-104 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 73-78 17397188-1 2007 Elongation factor Tu (EF-Tu) belongs to the family of GTP-binding proteins and requires elongation factor Ts (EF-Ts) for nucleotide exchange. Guanosine Triphosphate 54-57 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 17042495-0 2006 Delayed release of inorganic phosphate from elongation factor Tu following GTP hydrolysis on the ribosome. Guanosine Triphosphate 75-78 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 44-64 17033963-4 2006 EFTs functions as a guanine nucleotide exchange factor for EFTu, another translation elongation factor that brings aminoacylated transfer RNAs to the ribosomal A site as a ternary complex with guanosine triphosphate. Guanosine Triphosphate 193-215 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 59-63 17042495-3 2006 It was found that P(i) release from EF-Tu is >20-fold slower than GTP cleavage and limits the rate of the conformational switch of EF-Tu from the GTP- to the GDP-bound form. Guanosine Triphosphate 149-152 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 36-41 17042495-3 2006 It was found that P(i) release from EF-Tu is >20-fold slower than GTP cleavage and limits the rate of the conformational switch of EF-Tu from the GTP- to the GDP-bound form. Guanosine Triphosphate 149-152 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 134-139 16876786-2 2006 Kirromycin and enacyloxin block EF-Tu.GDP on the ribosome; pulvomycin and GE2270 A inhibit the interaction of EF-Tu.GTP with aa-tRNA. Guanosine Triphosphate 116-119 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 110-115 11373622-1 2001 In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1Balpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 145-150 16717093-5 2006 The effects are attributed to the interference of the mutations with the EF-Ts-induced movements of the P-loop of EF-Tu and changes at the domain 1/3 interface, leading to the release of the beta-phosphate group of GTP/GDP. Guanosine Triphosphate 215-218 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-119 16717093-6 2006 The K(d) for GTP is increased by more than 40 times when His-118 is replaced with Glu, which may explain the inhibition by His-118 mutations of aminoacyl-tRNA binding to EF-Tu. Guanosine Triphosphate 13-16 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 170-175 16601123-0 2006 SmpB triggers GTP hydrolysis of elongation factor Tu on ribosomes by compensating for the lack of codon-anticodon interaction during trans-translation initiation. Guanosine Triphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 32-52 16601123-5 2006 Based on these results, we suggest that SmpB structurally mimics the anticodon arm of tRNA and elicits GTP hydrolysis of EF-Tu upon tmRNA accommodation in the A site of the ribosome. Guanosine Triphosphate 103-106 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 121-126 15680978-3 2005 The ribosome recognizes aa-tRNA through shape discrimination of the codon-anticodon duplex and regulates the rates of GTP hydrolysis by EF-Tu and aa-tRNA accommodation in the A site by an induced fit mechanism. Guanosine Triphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 136-141 15581367-2 2004 The antibiotic pulvomycin is an inhibitor of protein synthesis that prevents the formation of the ternary complex between elongation factor (EF-) Tu.GTP and aminoacyl-tRNA. Guanosine Triphosphate 149-152 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 122-148 15581367-4 2004 Pulvomycin markedly affects the equilibrium and kinetics of the EF-Tu-nucleotide interaction, particularly of the EF-Tu.GTP complex. Guanosine Triphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 64-69 15581367-4 2004 Pulvomycin markedly affects the equilibrium and kinetics of the EF-Tu-nucleotide interaction, particularly of the EF-Tu.GTP complex. Guanosine Triphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-119 15581367-5 2004 The binding affinity of EF-Tu for GTP is increased 1000 times, mainly as the consequence of a dramatic decrease in the dissociation rate of this complex. Guanosine Triphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 24-29 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Triphosphate 169-172 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-113 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Triphosphate 169-172 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 192-197 15317456-2 2004 On the basis of available biochemical and structural evidence and results from molecular dynamics simulations, a model is proposed that accounts for the strong and selective binding of these compounds to human elongation factor eEF1A in the presence of GTP. Guanosine Triphosphate 253-256 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 228-233 15317456-3 2004 We suggest that the p-methoxyphenyl ring of these cyclic depsipeptides is inserted into the same pocket in eEF1A that normally lodges either the 3" terminal adenine of aminoacylated tRNA, as inferred from two prokaryotic EF-Tu.GTP.tRNA complexes, or the aromatic side chain of Phe/Tyr-163 from the nucleotide exchange factor eEF1Balpha, as observed in several X-ray crystal structures of a yeast eEF1A:eEF1Balpha complex. Guanosine Triphosphate 227-230 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 107-112 15317456-6 2004 In the GDP-bound form of eEF1A, this binding site exists only as two separate halves, which accounts for the much greater affinity of didemnins for the GTP-bound form of this elongation factor. Guanosine Triphosphate 152-155 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 25-30 15004548-5 2004 Streptomycin altered the rates of GTP hydrolysis by elongation factor Tu (EF-Tu) on cognate and near-cognate codons, resulting in almost identical rates of GTP hydrolysis and virtually complete loss of selectivity. Guanosine Triphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-72 15004548-5 2004 Streptomycin altered the rates of GTP hydrolysis by elongation factor Tu (EF-Tu) on cognate and near-cognate codons, resulting in almost identical rates of GTP hydrolysis and virtually complete loss of selectivity. Guanosine Triphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 15004548-5 2004 Streptomycin altered the rates of GTP hydrolysis by elongation factor Tu (EF-Tu) on cognate and near-cognate codons, resulting in almost identical rates of GTP hydrolysis and virtually complete loss of selectivity. Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-72 15004548-5 2004 Streptomycin altered the rates of GTP hydrolysis by elongation factor Tu (EF-Tu) on cognate and near-cognate codons, resulting in almost identical rates of GTP hydrolysis and virtually complete loss of selectivity. Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 12618188-1 2003 The highly abundant GTP binding protein elongation factor Tu (EF-Tu) fulfills multiple roles in bacterial protein biosynthesis. Guanosine Triphosphate 20-23 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-60 12618188-1 2003 The highly abundant GTP binding protein elongation factor Tu (EF-Tu) fulfills multiple roles in bacterial protein biosynthesis. Guanosine Triphosphate 20-23 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 62-67 11524957-3 2001 The concept of the shuttle role of elongation factor eEF1A is grounded; the factor, being in a GTP-bound form, delivers aminoacyl-tRNA to the ribosome and then, in the GDP form after hydrolysis of GTP on the ribosome, forms a complex with the deacylated tRNA and delivers it to the aminoacyl-tRNA synthetase. Guanosine Triphosphate 95-98 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 11524957-3 2001 The concept of the shuttle role of elongation factor eEF1A is grounded; the factor, being in a GTP-bound form, delivers aminoacyl-tRNA to the ribosome and then, in the GDP form after hydrolysis of GTP on the ribosome, forms a complex with the deacylated tRNA and delivers it to the aminoacyl-tRNA synthetase. Guanosine Triphosphate 197-200 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 15109577-5 2004 The eEF1A.GDP and eEF1A.GTP complexes were shown to be similar in their effect on the phenylalanyl-tRNA synthetase renaturation. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 4-9 15109577-5 2004 The eEF1A.GDP and eEF1A.GTP complexes were shown to be similar in their effect on the phenylalanyl-tRNA synthetase renaturation. Guanosine Triphosphate 24-27 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 18-23 16120370-1 2004 Elongation factor Tu (EF-Tu) binds GTP and aminoacyl-tRNA (aa-tRNA) forming a ternary complex which is delivered to the A-site of the ribosome. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 16120370-1 2004 Elongation factor Tu (EF-Tu) binds GTP and aminoacyl-tRNA (aa-tRNA) forming a ternary complex which is delivered to the A-site of the ribosome. Guanosine Triphosphate 35-38 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 15033564-3 2004 We have now demonstrated that minus strand synthesis is strongly repressed upon the binding of eEF1A.GTP to the valylated viral RNA. Guanosine Triphosphate 101-104 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 95-100 15033564-5 2004 Higher eEF1A.GTP levels were needed to repress minus strand synthesis templated by valyl-EMV TLS RNA, which binds eEF1A.GTP with lower affinity than does valyl-TYMV RNA. Guanosine Triphosphate 13-16 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 7-12 15033564-5 2004 Higher eEF1A.GTP levels were needed to repress minus strand synthesis templated by valyl-EMV TLS RNA, which binds eEF1A.GTP with lower affinity than does valyl-TYMV RNA. Guanosine Triphosphate 13-16 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-119 15033564-5 2004 Higher eEF1A.GTP levels were needed to repress minus strand synthesis templated by valyl-EMV TLS RNA, which binds eEF1A.GTP with lower affinity than does valyl-TYMV RNA. Guanosine Triphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 7-12 15033564-5 2004 Higher eEF1A.GTP levels were needed to repress minus strand synthesis templated by valyl-EMV TLS RNA, which binds eEF1A.GTP with lower affinity than does valyl-TYMV RNA. Guanosine Triphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-119 15033564-6 2004 Repression by eEF1A.GTP was also observed with a methionylated variant of TYMV RNA and with aminoacylated tRNAHis, tRNAAla, and tRNAPhe transcripts. Guanosine Triphosphate 20-23 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 14-19 15033564-7 2004 It is proposed that minus strand repression by eEF1A.GTP binding occurs early during infection to help coordinate the competing translation and replication functions of the genomic RNA. Guanosine Triphosphate 53-56 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 47-52 11991996-3 2002 The TLS of tobamoviral RNAs can be specifically aminoacylated and, in this state, can interact with eukaryotic elongation factor 1A (eEF1A)/GTP with high affinity. Guanosine Triphosphate 140-143 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 100-131 11991996-3 2002 The TLS of tobamoviral RNAs can be specifically aminoacylated and, in this state, can interact with eukaryotic elongation factor 1A (eEF1A)/GTP with high affinity. Guanosine Triphosphate 140-143 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 133-138 11991996-4 2002 Using a UV cross-linking assay, we detected another specific binding site for eEF1A/GTP, within the UPDs of TMV and crucifer-infecting tobamovirus (crTMV), that does not require aminoacylation. Guanosine Triphosphate 84-87 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 78-83 12370014-6 2002 GTP-hydrolysis induces a drastic conformational change in elongation factor (EF) Tu, which enables it to dissociate from the ribosome after having successfully delivered aminoacylated tRNA into the A-site. Guanosine Triphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 58-83 9553081-5 1998 When eEF1A binds to F-actin, there is a 7-fold decrease in the affinity for guanine nucleotide and an increase of 35% in the rate of GTP hydrolysis. Guanosine Triphosphate 133-136 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 5-10 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 15-18 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 81-90 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 15-18 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 144-153 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 81-90 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 144-153 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 81-90 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 144-153 11045624-7 2000 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Triphosphate 18-21 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-36 11045624-7 2000 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Triphosphate 18-21 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-32 11266545-1 2001 Eukaryotic elongation factor 1 (eEF-1) contains the guanine nucleotide exchange factor eEF-1B that loads the G protein eEF-1A with GTP after each cycle of elongation during protein synthesis. Guanosine Triphosphate 131-134 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-30 11266545-1 2001 Eukaryotic elongation factor 1 (eEF-1) contains the guanine nucleotide exchange factor eEF-1B that loads the G protein eEF-1A with GTP after each cycle of elongation during protein synthesis. Guanosine Triphosphate 131-134 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 32-37 11266545-1 2001 Eukaryotic elongation factor 1 (eEF-1) contains the guanine nucleotide exchange factor eEF-1B that loads the G protein eEF-1A with GTP after each cycle of elongation during protein synthesis. Guanosine Triphosphate 131-134 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 119-125 10647810-9 2000 Raising the assay temperature from 4 to 37 degrees C causes a 30-fold increase of Kd for EF-Tu x GTP x Phe-tRNA complexes. Guanosine Triphosphate 97-100 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 89-94 9553081-6 1998 Based upon our results and the relevant cellular concentrations, the predominant form of cellular eEF1A is calculated to be GTP.eEF1A.F-actin. Guanosine Triphosphate 124-127 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 9553081-6 1998 Based upon our results and the relevant cellular concentrations, the predominant form of cellular eEF1A is calculated to be GTP.eEF1A.F-actin. Guanosine Triphosphate 124-127 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 128-133 9553081-7 1998 We conclude that F-actin does not significantly modulate the basal enzymatic properties of eEF1A; however, actin may still influence protein synthesis by sequestering GTP.eEF1A away from interactions with its known translational ligands, e.g. aminoacyl-tRNA and ribosomes. Guanosine Triphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 171-176 9177487-10 1997 Sucrose gradient analysis indicates that the binding of EF-Tu(mt) to ribosomes can be detected in the presence of Phe-tRNA and a non-hydrolyzable analog of GTP. Guanosine Triphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 56-61 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Triphosphate 280-283 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 161-166 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Triphosphate 280-283 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Triphosphate 280-283 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Triphosphate 280-283 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-6 1997 The small-angle X-ray scattering study described here was undertaken to ascertain if the form of EF-G that has high ribosome affinity, EF-G.GTP, the structure of which is unknown, could be a mimic of EF-Tu.GDP. Guanosine Triphosphate 140-143 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 200-205 10397336-8 1998 The structural results provide a rather complete picture of the major structural forms of EF-Tu, including the so called ternary complex of aa-tRNA:EF-Tu:GTP. Guanosine Triphosphate 154-157 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 90-95 10397336-8 1998 The structural results provide a rather complete picture of the major structural forms of EF-Tu, including the so called ternary complex of aa-tRNA:EF-Tu:GTP. Guanosine Triphosphate 154-157 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 148-153