PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2470511-5 1989 When the EF-Tu.GTP.aminoacyl-tRNA ternary complex is bound to the ribosome, no tRNA-dependent A site protections are detected in 23S rRNA until EF-Tu is released. Guanosine Triphosphate 15-18 Tu translation elongation factor, mitochondrial Homo sapiens 9-14 2684669-6 1989 Our results show that the conformational transitions induced by the mutation strongly favor the regeneration of the active complex EF-TuG20.GTP, almost as effectively as with wild-type EF-Tu in the presence of elongation factor Ts. Guanosine Triphosphate 140-143 Tu translation elongation factor, mitochondrial Homo sapiens 131-139 2684669-6 1989 Our results show that the conformational transitions induced by the mutation strongly favor the regeneration of the active complex EF-TuG20.GTP, almost as effectively as with wild-type EF-Tu in the presence of elongation factor Ts. Guanosine Triphosphate 140-143 Tu translation elongation factor, mitochondrial Homo sapiens 131-136 2684669-9 1989 Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 22-30 2684669-9 1989 Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 22-27 2684669-10 1989 The ability of the ribosome to activate the EF-TuG20 center for GTP hydrolysis is strongly decreased, while the stimulation by aminoacyl-tRNA is conserved. Guanosine Triphosphate 64-67 Tu translation elongation factor, mitochondrial Homo sapiens 44-52 2684669-12 1989 The impaired activity of EF-TuG20 in poly(Phe) synthesis is related to the degree of defective GTP hydrolysis and, most interestingly, it is characterized by a striking increase of the fidelity of translation at high MgCl2 concentration. Guanosine Triphosphate 95-98 Tu translation elongation factor, mitochondrial Homo sapiens 25-33 2470511-5 1989 When the EF-Tu.GTP.aminoacyl-tRNA ternary complex is bound to the ribosome, no tRNA-dependent A site protections are detected in 23S rRNA until EF-Tu is released. Guanosine Triphosphate 15-18 Tu translation elongation factor, mitochondrial Homo sapiens 144-149 3122844-3 1987 All of the five known misreading-inducing antibiotics that were tested stabilised the binding of Phe-tRNAPhe after its affixture to the A site by EF-Tu with GTP hydrolysis. Guanosine Triphosphate 157-160 Tu translation elongation factor, mitochondrial Homo sapiens 146-151 2516316-2 1989 Similarities in function and amino acid sequence indicate that EF-Tu, p21ras, and G protein alpha-chains evolved from a primordial GTP-binding protein. Guanosine Triphosphate 131-134 Tu translation elongation factor, mitochondrial Homo sapiens 63-68 2516316-7 1989 A second class of GTPase inhibiting mutations in alpha s occurs in the codon for an Arg residue whose covalent modification by cholera toxin also inhibits GTP hydrolysis by alpha s. This Arg residue is located in a domain of alpha s not represented in EF-Tu or p21ras. Guanosine Triphosphate 18-21 Tu translation elongation factor, mitochondrial Homo sapiens 252-257 2516316-8 1989 We propose that this domain constitutes an intrinsic activator of GTP hydrolysis, and that it performs a function analogous to that performed for EF-Tu by the programmed ribosome and for p21ras by the recently discovered GTPase-activating protein. Guanosine Triphosphate 66-69 Tu translation elongation factor, mitochondrial Homo sapiens 146-151 3142522-3 1988 We were unable to find any consistent alteration produced by these antibiotics on coupled and uncoupled EF-G- and EF-Tu-dependent GTPases, on the EF-Tu-directed binding of aminoacyl-tRNA to ribosomes, and on the EF-G- and GTP-mediated translocation of peptidyl-tRNA bound to poly(U,C).ribosome complexes. Guanosine Triphosphate 130-133 Tu translation elongation factor, mitochondrial Homo sapiens 114-119 3888260-1 1985 We have investigated the formation of the aa-tRNA X EF-Tu X GTP ternary complex spectroscopically by monitoring a fluorescence change that accompanies the association of EF-Tu X GTP with Phe-tRNAPhe-F8, a functionally active analogue of Phe-tRNAPhe with a fluorescein moiety covalently attached to the s4U-8 base. Guanosine Triphosphate 60-63 Tu translation elongation factor, mitochondrial Homo sapiens 52-57 3014498-8 1986 EF-Tu X GTP thus treated has lost its ability to protect the ester bond of aminoacyl-tRNA. Guanosine Triphosphate 8-11 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 3510907-0 1986 The excess GTP hydrolyzed during mistranslation is expended at the stage of EF-Tu-promoted binding of non-cognate aminoacyl-tRNA. Guanosine Triphosphate 11-14 Tu translation elongation factor, mitochondrial Homo sapiens 76-81 3510907-1 1986 The system of translation of Sepharose-bound poly(U) in which all ribosomes are active in peptide elongation was used to determine the stoichiometry of GTP hydrolysis at the stage of EF-Tu-promoted aminoacyl-tRNA binding. Guanosine Triphosphate 152-155 Tu translation elongation factor, mitochondrial Homo sapiens 183-188 3510907-3 1986 It was demonstrated directly that the excess GTP hydrolyzed during misreading [(1984) FEBS Letters 178, 283-287] is expended at the stage of Ef-Tu-promoted binding of non-cognate aminoacyl-tRNA. Guanosine Triphosphate 45-48 Tu translation elongation factor, mitochondrial Homo sapiens 141-146 3902505-5 1985 The conclusion has been made that streptomycin blocks the stage of correction ("proof-reading") following GTP hydrolysis during EF-Tu-dependent aminoacyl-tRNA binding. Guanosine Triphosphate 106-109 Tu translation elongation factor, mitochondrial Homo sapiens 128-133 4044568-1 1985 Elongation factor Ts (EF-Ts) catalyzes the reaction EF-Tu X GDP + nucleotide diphosphate (NDP) reversible EF-Tu X NDP + GDP where NDP is GDP, IDP, GTP, or GMP X PCP. Guanosine Triphosphate 147-150 Tu translation elongation factor, mitochondrial Homo sapiens 52-57 4044568-1 1985 Elongation factor Ts (EF-Ts) catalyzes the reaction EF-Tu X GDP + nucleotide diphosphate (NDP) reversible EF-Tu X NDP + GDP where NDP is GDP, IDP, GTP, or GMP X PCP. Guanosine Triphosphate 147-150 Tu translation elongation factor, mitochondrial Homo sapiens 106-111 4044568-6 1985 The maximal rates of exchange of GDP and GTP are the same, which indicates that the rates of dissociation of EF-Ts from EF-Tu X GDP and EF-Tu X GTP are the same. Guanosine Triphosphate 144-147 Tu translation elongation factor, mitochondrial Homo sapiens 136-141 3888260-1 1985 We have investigated the formation of the aa-tRNA X EF-Tu X GTP ternary complex spectroscopically by monitoring a fluorescence change that accompanies the association of EF-Tu X GTP with Phe-tRNAPhe-F8, a functionally active analogue of Phe-tRNAPhe with a fluorescein moiety covalently attached to the s4U-8 base. Guanosine Triphosphate 60-63 Tu translation elongation factor, mitochondrial Homo sapiens 170-175 3888260-1 1985 We have investigated the formation of the aa-tRNA X EF-Tu X GTP ternary complex spectroscopically by monitoring a fluorescence change that accompanies the association of EF-Tu X GTP with Phe-tRNAPhe-F8, a functionally active analogue of Phe-tRNAPhe with a fluorescein moiety covalently attached to the s4U-8 base. Guanosine Triphosphate 178-181 Tu translation elongation factor, mitochondrial Homo sapiens 52-57 3888260-1 1985 We have investigated the formation of the aa-tRNA X EF-Tu X GTP ternary complex spectroscopically by monitoring a fluorescence change that accompanies the association of EF-Tu X GTP with Phe-tRNAPhe-F8, a functionally active analogue of Phe-tRNAPhe with a fluorescein moiety covalently attached to the s4U-8 base. Guanosine Triphosphate 178-181 Tu translation elongation factor, mitochondrial Homo sapiens 170-175 3888260-8 1985 The affinities of unmodified aa-tRNAs for EF-Tu X GTP were determined by their abilities to compete with the fluorescent aa-tRNA for binding to the protein. Guanosine Triphosphate 50-53 Tu translation elongation factor, mitochondrial Homo sapiens 42-47 6430701-0 1984 Modification of amino groups in EF-Tu.GTP and the ternary complex EF-Tu.GTP.valyl-tRNAVal. Guanosine Triphosphate 38-41 Tu translation elongation factor, mitochondrial Homo sapiens 32-37 6430701-0 1984 Modification of amino groups in EF-Tu.GTP and the ternary complex EF-Tu.GTP.valyl-tRNAVal. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 66-71 6551178-2 1983 The association of aminoacyl-tRNA (aa-tRNA) with elongation factor Tu.GTP to form an aa-tRNA.EF-Tu.GTP ternary complex was investigated by using two different fluorescent probes, both of which monitored structural changes near the juncture of the two arms of the L-shaped tRNA. Guanosine Triphosphate 70-73 Tu translation elongation factor, mitochondrial Homo sapiens 93-98 6551178-2 1983 The association of aminoacyl-tRNA (aa-tRNA) with elongation factor Tu.GTP to form an aa-tRNA.EF-Tu.GTP ternary complex was investigated by using two different fluorescent probes, both of which monitored structural changes near the juncture of the two arms of the L-shaped tRNA. Guanosine Triphosphate 99-102 Tu translation elongation factor, mitochondrial Homo sapiens 93-98 6551178-4 1983 However, when EF-Tu.GTP bound to Phe-tRNAPhe-F8, the emission intensity increased by approximately 30%, depending upon the solvent conditions. Guanosine Triphosphate 20-23 Tu translation elongation factor, mitochondrial Homo sapiens 14-19 6551178-8 1983 Instead, the binding of EF-Tu.GTP to the aa-tRNA resulted in a conformational change in the aa-tRNA near s4U-8. Guanosine Triphosphate 30-33 Tu translation elongation factor, mitochondrial Homo sapiens 24-29 6551178-11 1983 These results indicate that only the acceptor-T psi C arm of aa-tRNA interacts directly with EF-Tu.GTP and that the anticodon-D arm is available for direct interaction with the ribosome during recognition. Guanosine Triphosphate 99-102 Tu translation elongation factor, mitochondrial Homo sapiens 93-98 6751396-6 1982 Azidoaryl analogs of GTP and GDP as well as the chloroethylaminoaryl analog of GTP compete with GDP in the formation of the binary complex EF-Tu.GDP with the respective Ki values 3.9.10(-7) M (I), 2.9.10(-8)M (II), 6.9.10(-7)M (III), 5.0.10(-7)M (IV) and 3.8.10(-8)M (V) relative to GDP. Guanosine Triphosphate 21-24 Tu translation elongation factor, mitochondrial Homo sapiens 139-144 6819001-0 1982 Stabilization of the ternary complex EF-Tu.GTP.valyl-tRNAval by ammonium salts. Guanosine Triphosphate 43-46 Tu translation elongation factor, mitochondrial Homo sapiens 37-42 6819001-1 1982 In a search for crystallizing conditions for the ternary complex EF-Tu.GTP.valyl-tRNAval, the influence of various salts on its stability has been examined by measuring the rate of deacylation of the aminoacyl-tRNA in the complex. Guanosine Triphosphate 71-74 Tu translation elongation factor, mitochondrial Homo sapiens 65-70 6750613-1 1982 Guanosine 5"-[gamma-thio]triphosphate (GTP[gamma S] ) forms a stable ternary complex with polypeptide chain elongation factor Tu (EF-Tu) and aminoacyl-tRNA, and this complex binds rapidly and tightly to a properly programmed ribosome. Guanosine Triphosphate 39-42 Tu translation elongation factor, mitochondrial Homo sapiens 130-135 7032588-3 1981 Ternary complex formation with EF-Tu.GTP favors L-Tyr-tRNA by a factor greater than 25. Guanosine Triphosphate 37-40 Tu translation elongation factor, mitochondrial Homo sapiens 31-36 6751396-0 1982 Interaction of elongation factor EF-Tu with gamma-amides of GTP and beta-amides of GDP bearing the azidoaryl group or the chloroethylaminoaryl group placed at the terminal phosphate. Guanosine Triphosphate 60-63 Tu translation elongation factor, mitochondrial Homo sapiens 33-38 6751396-6 1982 Azidoaryl analogs of GTP and GDP as well as the chloroethylaminoaryl analog of GTP compete with GDP in the formation of the binary complex EF-Tu.GDP with the respective Ki values 3.9.10(-7) M (I), 2.9.10(-8)M (II), 6.9.10(-7)M (III), 5.0.10(-7)M (IV) and 3.8.10(-8)M (V) relative to GDP. Guanosine Triphosphate 79-82 Tu translation elongation factor, mitochondrial Homo sapiens 139-144 6751396-9 1982 GTP analogs I, II and V were found to substitute GTP in the stimulation of EF-Tu-dependent binding of aminoacyl-tRNA to the ribosome-mRNA complex. Guanosine Triphosphate 0-3 Tu translation elongation factor, mitochondrial Homo sapiens 75-80 6751396-9 1982 GTP analogs I, II and V were found to substitute GTP in the stimulation of EF-Tu-dependent binding of aminoacyl-tRNA to the ribosome-mRNA complex. Guanosine Triphosphate 49-52 Tu translation elongation factor, mitochondrial Homo sapiens 75-80 6108958-5 1981 GTP in its substrate requirements, in its involving EFTu . Guanosine Triphosphate 0-3 Tu translation elongation factor, mitochondrial Homo sapiens 52-56 30107527-2 2018 Cognate codon-anticodon interaction stimulates GTP hydrolysis within EF-Tu. Guanosine Triphosphate 47-50 Tu translation elongation factor, mitochondrial Homo sapiens 69-74 939763-19 1976 The kinetic studies on the reaction of ANM with EF-Tu before and after tryptic digestion indicated that both Fragment A and the hybrid molecule reacted with ANM in the presence of GTP three to four times more rapidly than in the presence of GDP. Guanosine Triphosphate 180-183 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 32612237-5 2020 GTP hydrolysis enables the GTPase domain of EF-Tu to extend away, releasing EF-Tu from tRNA. Guanosine Triphosphate 0-3 Tu translation elongation factor, mitochondrial Homo sapiens 44-49 32612237-5 2020 GTP hydrolysis enables the GTPase domain of EF-Tu to extend away, releasing EF-Tu from tRNA. Guanosine Triphosphate 0-3 Tu translation elongation factor, mitochondrial Homo sapiens 76-81 32061931-6 2020 Using structure-based and explicit solvent molecular dynamics simulations based on recent cryo-electron microscopy reconstructions, we studied the conformational change of EF-Tu from the guanosine triphosphate to guanine diphosphate conformation during aa-tRNA accommodation. Guanosine Triphosphate 187-209 Tu translation elongation factor, mitochondrial Homo sapiens 172-177 4551986-1 1972 The binding of elongation factor EF G to ribosomes inhibits the subsequent reaction of the ribosomes with the ternary complex aminoacyl-tRNA.EF Tu.GTP. Guanosine Triphosphate 147-150 Tu translation elongation factor, mitochondrial Homo sapiens 141-146 33280582-6 2020 Here, we present a contemporary view on the mechanism of GTPase activation and GTP hydrolysis by the elongation factors EF-Tu, EF-G, and SelB based on the analysis of structural, biochemical, and bioinformatics data. Guanosine Triphosphate 57-60 Tu translation elongation factor, mitochondrial Homo sapiens 120-125 30412578-6 2018 In particular, dissection of the cross-correlations of atomic displacements in both the GTP and GDP-bound states of Ras, transducin and elongation factor EF-Tu reveals analogous dynamic features. Guanosine Triphosphate 88-91 Tu translation elongation factor, mitochondrial Homo sapiens 154-159 30107527-3 2018 It has been proposed that EF-Tu undergoes a large conformational change subsequent to GTP hydrolysis, which results in the accommodation of aminoacyl-tRNA into the ribosomal A-site. Guanosine Triphosphate 86-89 Tu translation elongation factor, mitochondrial Homo sapiens 26-31 30107527-6 2018 Our studies show that GTP hydrolysis initiates a partial, comparatively small conformational change of EF-Tu on the ribosome, not directly along the path from the solution "GTP" to the "GDP" structure. Guanosine Triphosphate 22-25 Tu translation elongation factor, mitochondrial Homo sapiens 103-108 26786136-7 2016 Head swiveling motions in the small subunit are observed in the EF-Tu bound structures that were trapped post GTP hydrolysis. Guanosine Triphosphate 110-113 Tu translation elongation factor, mitochondrial Homo sapiens 64-69 29733411-1 2018 The GTPase EF-Tu in ternary complex with GTP and aminoacyl-tRNA (aa-tRNA) promotes rapid and accurate delivery of cognate aa-tRNAs to the ribosomal A site. Guanosine Triphosphate 4-7 Tu translation elongation factor, mitochondrial Homo sapiens 11-16 29733411-3 2018 We used the GTPase-deficient EF-Tu variant H84A with native GTP, rather than non-cleavable GTP analogues, to trap a near-cognate ternary complex in high-resolution ribosomal complexes of varying codon-recognition accuracy. Guanosine Triphosphate 12-15 Tu translation elongation factor, mitochondrial Homo sapiens 29-34 29733411-3 2018 We used the GTPase-deficient EF-Tu variant H84A with native GTP, rather than non-cleavable GTP analogues, to trap a near-cognate ternary complex in high-resolution ribosomal complexes of varying codon-recognition accuracy. Guanosine Triphosphate 60-63 Tu translation elongation factor, mitochondrial Homo sapiens 29-34 28138068-7 2017 We present the mechanisms of GTPase activation and GTP hydrolysis of EF-Tu and SelB and summarize what is known about the accommodation of aa-tRNA on the ribosome after its release from the elongation factor. Guanosine Triphosphate 29-32 Tu translation elongation factor, mitochondrial Homo sapiens 69-74 26971860-5 2016 Recent data suggest the GTPase mechanism of EF-Tu and provide an insight in the catalysis of GTP hydrolysis by its unusual activator, the ribosome. Guanosine Triphosphate 24-27 Tu translation elongation factor, mitochondrial Homo sapiens 44-49 24671767-4 2014 All incorporations exhibited fast and slow phases, reflecting the equilibrium fraction of AA-tRNA in active ternary complex with EF-Tu:GTP before the incorporation reaction. Guanosine Triphosphate 135-138 Tu translation elongation factor, mitochondrial Homo sapiens 129-134 26888283-7 2016 The task of IF1 appears to be the prevention of untimely interference by ternary aminoacyl (aa)-tRNA elongation factor thermo unstable (EF-Tu) GTP complexes. Guanosine Triphosphate 143-146 Tu translation elongation factor, mitochondrial Homo sapiens 136-141 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 14-19 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 151-154 Tu translation elongation factor, mitochondrial Homo sapiens 14-19 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 151-154 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 151-154 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-1 2015 The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu GTP is converted to EF-Tu GDP, forms part of an aminoacyl(aa)-tRNA EF-Tu GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Guanosine Triphosphate 151-154 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 26338772-2 2015 Such binding, placing a portion of EF-Tu in contact with the GTPase Associated Center (GAC), is followed by GTP hydrolysis and Pi release, and results in formation of a pretranslocation (PRE) complex. Guanosine Triphosphate 61-64 Tu translation elongation factor, mitochondrial Homo sapiens 35-40 26338772-6 2015 These pathways correspond to either reversible EF-Tu GDP dissociation from the ribosome prior to the major conformational change in EF-Tu that follows GTP hydrolysis, or irreversible dissociation after or concomitant with this conformational change. Guanosine Triphosphate 151-154 Tu translation elongation factor, mitochondrial Homo sapiens 132-137 25731854-3 2015 In addition, the availability of an increasing number of crystal structures of translational GTPases such as EF-Tu and EF-G have made it possible to probe the molecular details of GTP hydrolysis on the ribosome. Guanosine Triphosphate 93-96 Tu translation elongation factor, mitochondrial Homo sapiens 109-114 25246654-0 2014 Rejection of tmRNA SmpB after GTP hydrolysis by EF-Tu on ribosomes stalled on intact mRNA. Guanosine Triphosphate 30-33 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 25126896-1 2014 The universally conserved translation elongation factor EF-Tu delivers aminoacyl(aa)-tRNA in the form of an aa-tRNA EF-Tu GTP ternary complex (TC) to the ribosome where it binds to the cognate mRNA codon within the ribosomal A-site, leading to formation of a pretranslocation (PRE) complex. Guanosine Triphosphate 122-125 Tu translation elongation factor, mitochondrial Homo sapiens 56-61 25126896-1 2014 The universally conserved translation elongation factor EF-Tu delivers aminoacyl(aa)-tRNA in the form of an aa-tRNA EF-Tu GTP ternary complex (TC) to the ribosome where it binds to the cognate mRNA codon within the ribosomal A-site, leading to formation of a pretranslocation (PRE) complex. Guanosine Triphosphate 122-125 Tu translation elongation factor, mitochondrial Homo sapiens 116-121 24778639-2 2014 It has structural and functional similarities to tRNA: it has an upper half of the tRNA-like structure, its 5" end is processed by RNase P, it has typical tRNA-specific base modifications, it is aminoacylated with alanine, it binds to EF-Tu after aminoacylation and it enters the ribosome with EF-Tu and GTP. Guanosine Triphosphate 304-307 Tu translation elongation factor, mitochondrial Homo sapiens 235-240 24778639-2 2014 It has structural and functional similarities to tRNA: it has an upper half of the tRNA-like structure, its 5" end is processed by RNase P, it has typical tRNA-specific base modifications, it is aminoacylated with alanine, it binds to EF-Tu after aminoacylation and it enters the ribosome with EF-Tu and GTP. Guanosine Triphosphate 304-307 Tu translation elongation factor, mitochondrial Homo sapiens 294-299 24572811-3 2014 Interactions between codon and anticodon lead to activation of the GTPase domain of EF-Tu and GTP hydrolysis. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 84-89 25515218-3 2015 Here we examine different possible pathways for GTP hydrolysis by EF-Tu through extensive computer simulations. Guanosine Triphosphate 48-51 Tu translation elongation factor, mitochondrial Homo sapiens 66-71 24671767-6 2014 This allowed estimation of the affinity of each AA-tRNA to EF-Tu:GTP during translation, showing about a 10-fold higher EF-Tu affinity for AA-tRNAs formed from the tRNA(AlaB) body than from the tRNA(PheB) body. Guanosine Triphosphate 65-68 Tu translation elongation factor, mitochondrial Homo sapiens 59-64 24671767-6 2014 This allowed estimation of the affinity of each AA-tRNA to EF-Tu:GTP during translation, showing about a 10-fold higher EF-Tu affinity for AA-tRNAs formed from the tRNA(AlaB) body than from the tRNA(PheB) body. Guanosine Triphosphate 65-68 Tu translation elongation factor, mitochondrial Homo sapiens 120-125 24671767-8 2014 In contrast, the swap to the tRNA(AlaB) body did not increase the fast phase fraction of N-methyl-Phe incorporation, suggesting that the slow incorporation of N-methyl-Phe had a different cause than low EF-Tu:GTP affinity. Guanosine Triphosphate 209-212 Tu translation elongation factor, mitochondrial Homo sapiens 203-208 20348441-4 2010 Our investigations also revealed that the C-terminal tail is not required for the events until GTP is hydrolyzed by EF-Tu in complex with tmRNA-SmpB. Guanosine Triphosphate 95-98 Tu translation elongation factor, mitochondrial Homo sapiens 116-121 24025161-8 2013 Equilibrium binding studies showed that the A55U mutation considerably inhibited the binding of the EF-Tu GTP tRNA ternary complex to the ribosome. Guanosine Triphosphate 106-109 Tu translation elongation factor, mitochondrial Homo sapiens 100-105 23057558-7 2012 Our unmodified tRNA(Phe) derivative adaptor charged with a large unnatural AA, biotinyl-lysine, had a very low affinity for EF-Tu:GTP, while the small unnatural AAs on the same tRNA body had essentially the same affinities to EF-Tu:GTP as natural AAs on this tRNA, but still 2-fold less than natural Phe-tRNA(Phe). Guanosine Triphosphate 130-133 Tu translation elongation factor, mitochondrial Homo sapiens 124-129 21212264-1 2011 The accurate decoding of the genetic information by the ribosome relies on the communication between the decoding center of the ribosome, where the tRNA anticodon interacts with the codon, and the GTPase center of EF-Tu, where GTP hydrolysis takes place. Guanosine Triphosphate 197-200 Tu translation elongation factor, mitochondrial Homo sapiens 214-219 21152913-8 2011 EF-Tu:GDP complex acquired a configuration different from that found in the crystal structure of EF-Tu with a GTP analogue, showing conformational changes in the switch I and II regions. Guanosine Triphosphate 110-113 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 21152913-8 2011 EF-Tu:GDP complex acquired a configuration different from that found in the crystal structure of EF-Tu with a GTP analogue, showing conformational changes in the switch I and II regions. Guanosine Triphosphate 110-113 Tu translation elongation factor, mitochondrial Homo sapiens 97-102 20215430-6 2010 Cleavage of SRL slightly affected binding of elongation factor Tu ternary complex (EF-Tu*GTP*tRNA) to the ribosome. Guanosine Triphosphate 89-92 Tu translation elongation factor, mitochondrial Homo sapiens 83-88 24345396-6 2014 We find that although mutation of His136 does not reduce SmpB"s affinity for the ribosomal A-site, it dramatically reduces the rate of GTP hydrolysis by EF-Tu. Guanosine Triphosphate 135-138 Tu translation elongation factor, mitochondrial Homo sapiens 153-158 17130126-5 2007 We demonstrate that recombinant EF-Tumt prevents thermal aggregation of proteins and enhances protein refolding in vitro and that this EF-Tumt chaperone activity proceeds in a GTP-independent manner. Guanosine Triphosphate 176-179 Tu translation elongation factor, mitochondrial Homo sapiens 32-39 19524667-0 2009 The R336Q mutation in human mitochondrial EFTu prevents the formation of an active mt-EFTu.GTP.aa-tRNA ternary complex. Guanosine Triphosphate 91-94 Tu translation elongation factor, mitochondrial Homo sapiens 42-46 19524667-0 2009 The R336Q mutation in human mitochondrial EFTu prevents the formation of an active mt-EFTu.GTP.aa-tRNA ternary complex. Guanosine Triphosphate 91-94 Tu translation elongation factor, mitochondrial Homo sapiens 86-90 19285947-4 2009 Here we show instead that aminoacyl-tRNAs in ternary complex with EF-Tu*GTP can readily dissociate and rebind to aminoacyl-tRNA synthetases. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 66-71 19104062-4 2009 Our results show that the slowest step in incorporation of N-alkylamino acids is accommodation/peptidyl transfer after GTP hydrolysis on EF-Tu. Guanosine Triphosphate 119-122 Tu translation elongation factor, mitochondrial Homo sapiens 137-142 17130126-5 2007 We demonstrate that recombinant EF-Tumt prevents thermal aggregation of proteins and enhances protein refolding in vitro and that this EF-Tumt chaperone activity proceeds in a GTP-independent manner. Guanosine Triphosphate 176-179 Tu translation elongation factor, mitochondrial Homo sapiens 135-142 15952884-2 2005 Recent biochemical and structural data make it possible to understand at least in outline the structural basis for tRNA selection, in which codon recognition by cognate tRNA results in the hydrolysis of GTP by EF-Tu over 75 A away. Guanosine Triphosphate 203-206 Tu translation elongation factor, mitochondrial Homo sapiens 210-215 16682558-1 2006 The interaction between the GTPase-associated center (GAC) and the aminoacyl-tRNA.EF-Tu.GTP ternary complex is of crucial importance in the dynamic process of decoding and tRNA accommodation. Guanosine Triphosphate 28-31 Tu translation elongation factor, mitochondrial Homo sapiens 82-87 16682558-5 2006 Two types of conformations of the L11-rRNA complex, produced by the simulations, match the cryo-EM maps representing the states either bound or unbound to the aa-tRNA.EF-Tu.GTP ternary complex. Guanosine Triphosphate 173-176 Tu translation elongation factor, mitochondrial Homo sapiens 167-172 16023674-8 2005 Second, the enzymic reactions of the ribosomal cycle (structural changes caused by transpeptidation and by GTP hydrolyses in EF-Tu and EF-G) disrupt kinetic traps that prevent tRNAs from dissociating into solution during their motion within the ribosome and are necessary for progression of the cycle. Guanosine Triphosphate 107-110 Tu translation elongation factor, mitochondrial Homo sapiens 125-130 16843583-5 2006 The reset energy would be provided in part, in the author"s mode, from GTP cleavage on a binary EF-Tu.GTP complex (BC). Guanosine Triphosphate 71-74 Tu translation elongation factor, mitochondrial Homo sapiens 96-101 16843583-5 2006 The reset energy would be provided in part, in the author"s mode, from GTP cleavage on a binary EF-Tu.GTP complex (BC). Guanosine Triphosphate 102-105 Tu translation elongation factor, mitochondrial Homo sapiens 96-101 16890341-4 2006 Information about the correctness of the anticodon must be sent from the decoding center to the elongation factor, EF-Tu, where the GTP hydrolysis takes place. Guanosine Triphosphate 132-135 Tu translation elongation factor, mitochondrial Homo sapiens 115-120 15952884-4 2005 Part of the additional binding energy of cognate tRNA is used to induce conformational changes in the ribosome that stabilize a transition state for GTP hydrolysis by EF-Tu and subsequently result in accelerated accommodation of tRNA into the peptidyl transferase center. Guanosine Triphosphate 149-152 Tu translation elongation factor, mitochondrial Homo sapiens 167-172 15952884-7 2005 However, many fundamental questions remain, such as the mechanism of activation of GTP hydrolysis by EF-Tu, and the relationship between decoding and frameshifting. Guanosine Triphosphate 83-86 Tu translation elongation factor, mitochondrial Homo sapiens 101-106 14550646-2 2003 Its amino-terminal three domains show homology to elongation factor EF-Tu and accordingly bind GTP and selenocysteyl-tRNASec. Guanosine Triphosphate 95-98 Tu translation elongation factor, mitochondrial Homo sapiens 68-73 17194938-5 2004 Elongation factors EF-Tu and EF-G with GTP are considered as catalysts of conformational transitions during aminoacyl-tRNA binding and translocation, and the theory of NTP-dependent conformational catalysis via conformational intermediates is discussed. Guanosine Triphosphate 39-42 Tu translation elongation factor, mitochondrial Homo sapiens 19-24 14715237-1 2004 An analysis is made of the rate constants for the reactions involving the interactions of EF-Tu, EF-Ts, GDP, and GTP recently derived by Gromadski et al. Guanosine Triphosphate 113-116 Tu translation elongation factor, mitochondrial Homo sapiens 90-95 14715237-4 2004 A kinetic scheme consistent with the thermodynamic barrier can be achieved by modification of various rate constants, particularly of those involving the release of EF-Ts from EF-Tu.GTP.EF-Ts, but such constants are markedly different from what are experimentally observed. Guanosine Triphosphate 182-185 Tu translation elongation factor, mitochondrial Homo sapiens 176-181 14622005-4 2003 Gln97 is located in the switch II region in the GDP/GTP binding domain of EF-Tu. Guanosine Triphosphate 52-55 Tu translation elongation factor, mitochondrial Homo sapiens 74-79 14622005-11 2003 The variant bound GTP at 3-fold lower levels than the wild-type EF-Tu. Guanosine Triphosphate 18-21 Tu translation elongation factor, mitochondrial Homo sapiens 64-69 10937868-4 2000 EF-Tu x GTP forms a ternary complex with aminoacyl-tRNA, which binds to the ribosome. Guanosine Triphosphate 8-11 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 12460565-1 2002 Translation of polyphenylalanine from a polyuridine template by the ribosome in the absence of the elongation factors EFG and EFTu (and the energy derived from GTP hydrolysis) is promoted by modification of the ribosome with thiol-specific reagents such as para-chloromercuribenzoate (pCMB). Guanosine Triphosphate 160-163 Tu translation elongation factor, mitochondrial Homo sapiens 126-130 12102560-1 2002 This review considers several aspects of the function of EF-Tu, a protein that has greatly contributed to the advancement of our knowledge of both protein biosynthesis and GTP-binding proteins in general. Guanosine Triphosphate 172-175 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 12023840-5 2002 These high-resolution glimpses into various ribosomal states together with a large body of biochemical data reveal an intricate interplay between the tRNAs and the three ribosomal binding sites, providing an explanation for the remarkable features of the ribosome, such as the ability to select the correct ternary complex aminoacyl-tRNA.EF-Tu.GTP out of more than 40 extremely similar tRNA complexes, the precise movement of the tRNA(2).mRNA complex during translocation and the maintenance of the reading frame. Guanosine Triphosphate 344-347 Tu translation elongation factor, mitochondrial Homo sapiens 338-343 11907568-6 2002 The proposed mechanisms are compatible with the known structures, conformations and functions of the ribosome and its component parts including tRNAs and EF-Tu, in both the GTP and GDP states. Guanosine Triphosphate 173-176 Tu translation elongation factor, mitochondrial Homo sapiens 154-159 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 61-66 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 67-70 Tu translation elongation factor, mitochondrial Homo sapiens 61-66 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 170-173 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 170-173 Tu translation elongation factor, mitochondrial Homo sapiens 61-66 11595738-5 2001 Deacylated tmRNA can form a complex with either EF-Tu.GDP or EF-Tu.GTP, the association constants are about one order of magnitude smaller than that of an Ala-tRNA.EF-Tu.GTP complex. Guanosine Triphosphate 170-173 Tu translation elongation factor, mitochondrial Homo sapiens 61-66 10801827-2 2000 This process requires the formation of a ternary complex (EF-Tu.GTP.aa-tRNA). Guanosine Triphosphate 64-67 Tu translation elongation factor, mitochondrial Homo sapiens 58-63 10801827-4 2000 Exchange of GDP for GTP is carried out through the formation of a complex with EF-Ts (EF-Tu.Ts). Guanosine Triphosphate 20-23 Tu translation elongation factor, mitochondrial Homo sapiens 86-91 10937868-5 2000 Only when a matching codon is recognized, the GTPase of EF-Tu is stimulated, rapid GTP hydrolysis and Pi release take place, EF-Tu rearranges to the GDP form, and aminoacyl-tRNA is released into the peptidyltransferase center. Guanosine Triphosphate 46-49 Tu translation elongation factor, mitochondrial Homo sapiens 56-61 10937868-5 2000 Only when a matching codon is recognized, the GTPase of EF-Tu is stimulated, rapid GTP hydrolysis and Pi release take place, EF-Tu rearranges to the GDP form, and aminoacyl-tRNA is released into the peptidyltransferase center. Guanosine Triphosphate 46-49 Tu translation elongation factor, mitochondrial Homo sapiens 125-130 10600553-1 1999 Using three-dimensional cryoelectron microscopy, the binding positions of tRNA and elongation factors EF-G and EF-Tu (the latter complexed with aminoacyl tRNA and GTP) on the ribosome were determined in previous studies. Guanosine Triphosphate 163-166 Tu translation elongation factor, mitochondrial Homo sapiens 111-116 9701288-2 1998 The factor has a GTP binding site and shows sequence similarity to elongation factors EF-Tu and EF-G. Guanosine Triphosphate 17-20 Tu translation elongation factor, mitochondrial Homo sapiens 86-91 9678602-4 1998 Since it mimics the structure of the ternary complex of EF-Tu:GTP with aminoacyl-tRNA, which subsequently binds to the ribosome, EF-G:GDP leaves an imprint on the ribosome for the ternary complex. Guanosine Triphosphate 62-65 Tu translation elongation factor, mitochondrial Homo sapiens 56-61 8805704-6 1996 Our data reveal that the GTP cycle of Rab proteins differs from that of other GTPases (for example, EF-Tu) and indicate that GTP hydrolysis acts as a timer that determines the frequency of membrane docking/fusion events. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 100-105 9405422-5 1997 Renaturation of rhodanese and GTP hydrolysis by EF-Tu are greatly enhanced by the guanine nucleotide exchange factor EF-Ts. Guanosine Triphosphate 30-33 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 9405422-9 1997 Kirromycin locks EF-Tu in the open conformation in the presence of either GTP or GDP, whereas pulvomycin locks the factor in the closed conformation. Guanosine Triphosphate 74-77 Tu translation elongation factor, mitochondrial Homo sapiens 17-22 8903506-3 1996 The protein synthesis elongation factor EF-Tu was the first G-protein whose nucleotide binding domain was solved structurally by X-ray crystallography to yield a structural definition of the GDP-bound form, but a still increasing number of new structures of G-proteins are appearing in the literature, in both GDP and GTP bound forms. Guanosine Triphosphate 318-321 Tu translation elongation factor, mitochondrial Homo sapiens 40-45 8768893-2 1996 The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined. Guanosine Triphosphate 71-74 Tu translation elongation factor, mitochondrial Homo sapiens 65-70 8955901-2 1996 Of the prokaryotic translational factors, IF2, EF-Tu, SELB, EF-G and RF3 are GTP-binding proteins. Guanosine Triphosphate 77-80 Tu translation elongation factor, mitochondrial Homo sapiens 47-52 7925958-0 1994 Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP. Guanosine Triphosphate 88-91 Tu translation elongation factor, mitochondrial Homo sapiens 82-87 8749370-3 1995 In the field of elongation factors (EFs), three very important structures have been determined: EF-G, the ternary complex of EF-Tu.GTP with aminoacyl-tRNA, and the EF-Tu.EF-Ts complex. Guanosine Triphosphate 131-134 Tu translation elongation factor, mitochondrial Homo sapiens 125-130 8749358-3 1995 In addition, the complex of EF-Tu with a GTP analogue and Phe-tRNA(Phe) has a structure that overlaps exceedingly well with that of EF-G-GDP. Guanosine Triphosphate 41-44 Tu translation elongation factor, mitochondrial Homo sapiens 28-33 8722038-3 1995 The conformations of EF-G.GDP and EF-Tu.GTP are closely related. Guanosine Triphosphate 40-43 Tu translation elongation factor, mitochondrial Homo sapiens 34-39 8722038-4 1995 EF-Tu goes through a large conformational change upon GTP cleavage. Guanosine Triphosphate 54-57 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 8001671-0 1995 Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature. Guanosine Triphosphate 4-8 Tu translation elongation factor, mitochondrial Homo sapiens 25-30 8001671-1 1995 Recent observations indicate that the stoichiometry for the complex between EF-Tu.GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. Guanosine Triphosphate 82-85 Tu translation elongation factor, mitochondrial Homo sapiens 76-81 8001671-2 1995 At 37 degrees C two EF-Tu.GTPs bind one aa-tRNA in an extended ternary complex, but at 0 degrees C the complex has 1:1 stoichiometry. Guanosine Triphosphate 26-30 Tu translation elongation factor, mitochondrial Homo sapiens 20-25 8001671-3 1995 However, the present experiments show that there are two GTPs hydrolyzed on EF-Tu per peptide bond in poly(Phe) synthesis at 37 degrees C as well as at 0 degrees C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome. Guanosine Triphosphate 57-61 Tu translation elongation factor, mitochondrial Homo sapiens 76-81 7925958-3 1994 These have been mapped onto the 3D structures of EF-Tu.GTP and EF-Tu.GDP. Guanosine Triphosphate 55-58 Tu translation elongation factor, mitochondrial Homo sapiens 49-54 7925958-4 1994 In the active GTP form of EF-Tu the mutations cluster on each side of the interface between domains I and III. Guanosine Triphosphate 14-17 Tu translation elongation factor, mitochondrial Homo sapiens 26-31 7880651-6 1994 The larger domain of the 3D reconstruction is consistent in shape and size with the GTP-binding domains of EF-Tu and p21-RAS, while the smaller domain is compatible in structure with part of the peptide-binding protein calmodulin. Guanosine Triphosphate 84-87 Tu translation elongation factor, mitochondrial Homo sapiens 107-112 8076683-1 1994 Diversity before and unity after interaction with EF-Tu:GTP. Guanosine Triphosphate 56-59 Tu translation elongation factor, mitochondrial Homo sapiens 50-55 1537852-2 1992 Association constants were determined by Scatchard plot analysis (the constants are given in units of [10(7)/M] measured at 15 mM Mg2+): the ternary complex Phe-tRNA.elongation factor EF-Tu.GTP (12 +/- 3), Phe-tRNA (1 +/- 0.4), AcPhe-tRNA (0.7 +/- 0.3), and deacylated tRNA(Phe) (0.4 +/- 0.15) bind with decreasing affinity to the A site of poly(U)-programmed ribosomes. Guanosine Triphosphate 190-193 Tu translation elongation factor, mitochondrial Homo sapiens 184-189 8031905-0 1994 Two GTPs are hydrolysed on two molecules of EF-Tu for each elongation cycle during code translation. Guanosine Triphosphate 4-8 Tu translation elongation factor, mitochondrial Homo sapiens 44-49 8031905-1 1994 A new experimental design has been used to determine the number of GTPs hydrolysed per peptide bond in EF-Tu function in a poly(U)-translation system. Guanosine Triphosphate 67-71 Tu translation elongation factor, mitochondrial Homo sapiens 103-108 1503566-5 1992 Measurement of on and off rate constants for binding of GTP to EF-Tu.EF-Ts and of the affinity of EF-Ts for EF-Tu.GTP should prove of importance in resolving discrepancies. Guanosine Triphosphate 56-59 Tu translation elongation factor, mitochondrial Homo sapiens 63-68 1503566-5 1992 Measurement of on and off rate constants for binding of GTP to EF-Tu.EF-Ts and of the affinity of EF-Ts for EF-Tu.GTP should prove of importance in resolving discrepancies. Guanosine Triphosphate 114-117 Tu translation elongation factor, mitochondrial Homo sapiens 63-68 1503566-5 1992 Measurement of on and off rate constants for binding of GTP to EF-Tu.EF-Ts and of the affinity of EF-Ts for EF-Tu.GTP should prove of importance in resolving discrepancies. Guanosine Triphosphate 114-117 Tu translation elongation factor, mitochondrial Homo sapiens 108-113 1637866-2 1992 It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA.EF-Tu.GTP complex up to GTP hydrolysis stage on the ribosome. Guanosine Triphosphate 120-123 Tu translation elongation factor, mitochondrial Homo sapiens 114-119 1637866-2 1992 It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA.EF-Tu.GTP complex up to GTP hydrolysis stage on the ribosome. Guanosine Triphosphate 120-123 Tu translation elongation factor, mitochondrial Homo sapiens 114-119 1508161-0 1992 [Elongation factor EF-Ts interacts with the aminoacyl-tRNA.EF-Tu.GTP complex]. Guanosine Triphosphate 65-68 Tu translation elongation factor, mitochondrial Homo sapiens 59-64 1508161-1 1992 The fluorescence polarization technique has been used to study the interaction of the EF-Ts dansyl derivative with EF-Tu after nucleotide exchange and binding of the aminoacyl-tRNA to EF-Tu.GTP. Guanosine Triphosphate 190-193 Tu translation elongation factor, mitochondrial Homo sapiens 115-120 1508161-1 1992 The fluorescence polarization technique has been used to study the interaction of the EF-Ts dansyl derivative with EF-Tu after nucleotide exchange and binding of the aminoacyl-tRNA to EF-Tu.GTP. Guanosine Triphosphate 190-193 Tu translation elongation factor, mitochondrial Homo sapiens 184-189 1508161-2 1992 It is shown that the ternary complex formation results in the increase of EF-Ts affinity to EF-Tu and EF-Ts remains bound to EF-Tu up to the GTP hydrolysis stage on the ribosome. Guanosine Triphosphate 141-144 Tu translation elongation factor, mitochondrial Homo sapiens 92-97 1508161-2 1992 It is shown that the ternary complex formation results in the increase of EF-Ts affinity to EF-Tu and EF-Ts remains bound to EF-Tu up to the GTP hydrolysis stage on the ribosome. Guanosine Triphosphate 141-144 Tu translation elongation factor, mitochondrial Homo sapiens 125-130 1804111-1 1991 The kinetics of the heterologous exchange of GDP bound to EF-Tu by free GTP catalysed by EF-Ts have been analysed with a view to correlating results obtainable with different computational procedures. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 58-63 1959611-3 1991 As expected for these two distinct species, the dissociation of the EF-TuArBs.GTP complex in the presence of kirromycin shows a biphasic curve; in contrast, a monophasic GTP dissociation rate was found for a combination of two mutated EF-Tu species, EF-TuArBo, revealing the existence of intermolecular interactions. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 68-73 1959611-3 1991 As expected for these two distinct species, the dissociation of the EF-TuArBs.GTP complex in the presence of kirromycin shows a biphasic curve; in contrast, a monophasic GTP dissociation rate was found for a combination of two mutated EF-Tu species, EF-TuArBo, revealing the existence of intermolecular interactions. Guanosine Triphosphate 170-173 Tu translation elongation factor, mitochondrial Homo sapiens 68-73 1804111-4 1991 There is a close interrelationship between the constants for the binding of GTP to EF-Tu.EF-Ts and of EF-Ts to EF-Tu.GTP. Guanosine Triphosphate 76-79 Tu translation elongation factor, mitochondrial Homo sapiens 111-116 1804111-4 1991 There is a close interrelationship between the constants for the binding of GTP to EF-Tu.EF-Ts and of EF-Ts to EF-Tu.GTP. Guanosine Triphosphate 117-120 Tu translation elongation factor, mitochondrial Homo sapiens 83-88 1804111-4 1991 There is a close interrelationship between the constants for the binding of GTP to EF-Tu.EF-Ts and of EF-Ts to EF-Tu.GTP. Guanosine Triphosphate 117-120 Tu translation elongation factor, mitochondrial Homo sapiens 111-116 1804111-2 1991 The affinity of EF-Ts for EF-Tu.GTP was found to be somewhat less than previously proposed by Romero et al. Guanosine Triphosphate 32-35 Tu translation elongation factor, mitochondrial Homo sapiens 26-31 1804111-4 1991 There is a close interrelationship between the constants for the binding of GTP to EF-Tu.EF-Ts and of EF-Ts to EF-Tu.GTP. Guanosine Triphosphate 76-79 Tu translation elongation factor, mitochondrial Homo sapiens 83-88 1885567-4 1991 EF-Tu.Tsmt is capable of forming a ternary complex with GTP and Escherichia coli Phe-tRNA as demonstrated by gel filtration chromatography, nitrocellulose filter binding, and by protection of the aminoacyl-tRNA bond from hydrolysis. Guanosine Triphosphate 56-59 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 1885567-5 1991 GDP and the non-hydrolyzable GTP analog guanyl-5"-yl imidodiphosphate are also capable of facilitating ternary complex formation with EF-Tu.Tsmt, but are less effective. Guanosine Triphosphate 29-32 Tu translation elongation factor, mitochondrial Homo sapiens 134-139 1896033-0 1991 [Ef-Ts elongation factor interacts with elongation factor EF-Tu on ribosomes prior to the GTP hydrolysis stage]. Guanosine Triphosphate 90-93 Tu translation elongation factor, mitochondrial Homo sapiens 58-63 1742352-0 1991 The influence of tRNA located at the P-site on the turnover of EF-Tu.GTP on ribosomes. Guanosine Triphosphate 69-72 Tu translation elongation factor, mitochondrial Homo sapiens 63-68 1742352-1 1991 The turnover of EF-Tu.GTP on poly-U programmed ribosomes was measured both in the presence and in the absence of N-acetylated Phe-tRNA(Phe) at the P-site. Guanosine Triphosphate 22-25 Tu translation elongation factor, mitochondrial Homo sapiens 16-21 1742352-3 1991 In this reaction, the ribosome can be considered as an enzyme catalysing the transition of EF-Tu.GTP to EF-Tu.GTP. Guanosine Triphosphate 97-100 Tu translation elongation factor, mitochondrial Homo sapiens 91-96 1742352-3 1991 In this reaction, the ribosome can be considered as an enzyme catalysing the transition of EF-Tu.GTP to EF-Tu.GTP. Guanosine Triphosphate 97-100 Tu translation elongation factor, mitochondrial Homo sapiens 104-109 1742352-3 1991 In this reaction, the ribosome can be considered as an enzyme catalysing the transition of EF-Tu.GTP to EF-Tu.GTP. Guanosine Triphosphate 110-113 Tu translation elongation factor, mitochondrial Homo sapiens 91-96 1742352-3 1991 In this reaction, the ribosome can be considered as an enzyme catalysing the transition of EF-Tu.GTP to EF-Tu.GTP. Guanosine Triphosphate 110-113 Tu translation elongation factor, mitochondrial Homo sapiens 104-109 1742352-4 1991 A constant EF-Tu.GTP concentration is maintained by regenerating GDP to GTP at the expense of phosphoenolpyruvate by pyruvate kinase. Guanosine Triphosphate 17-20 Tu translation elongation factor, mitochondrial Homo sapiens 11-16 1742352-4 1991 A constant EF-Tu.GTP concentration is maintained by regenerating GDP to GTP at the expense of phosphoenolpyruvate by pyruvate kinase. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 11-16 1742352-6 1991 Ribosomes with an occupied P-site are more efficient in stimulating the GTPase of EF-Tu.GTP than ribosomes with an empty P-site. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 82-87 1742352-7 1991 The data suggest that this is mainly caused by an increased affinity of EF-Tu.GTP for ribosomes with a filled P-site rather than by an enhanced reactivity of the GTPase centre. Guanosine Triphosphate 78-81 Tu translation elongation factor, mitochondrial Homo sapiens 72-77 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 40-45 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 72-75 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 146-149 Tu translation elongation factor, mitochondrial Homo sapiens 40-45 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 146-149 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 1896033-2 1991 It is shown that EF-Ts dissociates from EF-Tu only after EF-Tu-mediated GTP hydrolysis, i.e. EF-Ts within the EF-Tu.ribosome complexes in the pre-GTP-hydrolysis state co-sediments with the ribosomes and its rate of proteolysis is distinct from that of free EF-Ts. Guanosine Triphosphate 146-149 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 2209587-1 1990 EF-Tu is often referred to as a model for guanine-nucleotide-binding regulatory proteins (G-proteins), since X-ray diffraction analysis of its GTP-binding domain shows a detailed location of the "consensus" amino acid sequences involved in nucleotide binding. Guanosine Triphosphate 143-146 Tu translation elongation factor, mitochondrial Homo sapiens 0-5 2209587-5 1990 By consequence, if indeed AlF4- behaves as a gamma-phosphate analogue in G-proteins, then EF-Tu must have a different GDP/GTP binding site, despite of the conserved consensus sequences. Guanosine Triphosphate 122-125 Tu translation elongation factor, mitochondrial Homo sapiens 90-95 2180702-4 1990 Second, kcat/Km for the interaction between the EF-Tu.GTP.aa-tRNA complex and the ribosome was decreased by the mutation to one third of its wild-type value. Guanosine Triphosphate 54-57 Tu translation elongation factor, mitochondrial Homo sapiens 48-53 2180702-5 1990 No differences were observed between mutant and wild-type factor in the regeneration of EF-Tu.GTP from EF-Tu.GDP via EF-Ts or in the mistranslation frequency by Leu-tRNA(4Leu). Guanosine Triphosphate 94-97 Tu translation elongation factor, mitochondrial Homo sapiens 103-108 2119552-1 1990 Structural, biochemical and molecular genetic studies of EF-Tu, p21ras and alpha s have begun to reveal the inner workings of the molecular machine used by these and other GTP-binding proteins. Guanosine Triphosphate 172-175 Tu translation elongation factor, mitochondrial Homo sapiens 57-62 2119552-2 1990 Further understanding of this molecular machine will ultimately come from crystal structures of the G protein alpha chains as well as from crystal structures of the GTP-bound forms of p21ras and EF-Tu. Guanosine Triphosphate 165-168 Tu translation elongation factor, mitochondrial Homo sapiens 195-200