PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 33046533-3 2020 Although the majority of the 1,157-nucleotide (nt) Saccharomyces cerevisiae telomerase RNA, TLC1, is rapidly evolving, the central catalytic core is largely conserved, containing the template, template-boundary helix, pseudoknot, and core-enclosing helix (CEH). 1,157-nucleotide 29-45 TLC1 Saccharomyces cerevisiae S288C 92-96 33046533-3 2020 Although the majority of the 1,157-nucleotide (nt) Saccharomyces cerevisiae telomerase RNA, TLC1, is rapidly evolving, the central catalytic core is largely conserved, containing the template, template-boundary helix, pseudoknot, and core-enclosing helix (CEH). nt 47-49 TLC1 Saccharomyces cerevisiae S288C 92-96 32121425-4 2020 Here, we first show that Sm7 can stabilize poly(A)- TLC1 even when its binding site is repositioned via circular permutation to several different positions within TLC1, further supporting the conclusion that the telomerase holoenzyme is organizationally flexible. Poly A 43-50 TLC1 Saccharomyces cerevisiae S288C 52-56 28637749-5 2017 In the presence of DSBs, TLC1 RNA remains nucleolar in most G2/M cells but accumulates in the nucleoplasm and colocalizes with DSBs in rad52Delta cells, leading to de novo telomere additions. dsbs 19-23 TLC1 Saccharomyces cerevisiae S288C 25-29 23610127-5 2013 To address this question, we localized the Ku-binding site of the TLC1 hairpin with single-nucleotide resolution using phosphorothioate footprinting, used chemical modification to identify an unpredicted motif within the hairpin secondary structure, and carried out mutagenesis of the stem-loop to ascertain the critical elements within the RNA that permit Ku binding. Parathion 119-135 TLC1 Saccharomyces cerevisiae S288C 66-70 16299517-3 2005 Here, we reduce the 1,157-nucleotide (nt) Saccharomyces cerevisiae TLC1 RNA to a size smaller than the 451-nt human RNA while retaining function in vivo. 1,157-nucleotide 20-36 TLC1 Saccharomyces cerevisiae S288C 67-71 18840651-2 2008 TLC1 shares several features with snRNA, among them the presence of a trimethylguanosine (m(3)G) cap structure at the 5" end of the RNA. trimethylguanosine 70-88 TLC1 Saccharomyces cerevisiae S288C 0-4 19875981-3 2010 Sas2 acetylates histone H4 lysine 16 (H4K16), and telomere shortening in tlc1 mutants was accompanied by a selective and Sas2-dependent increase in subtelomeric H4K16 acetylation. Lysine 27-33 TLC1 Saccharomyces cerevisiae S288C 73-77 15813705-4 2005 The GST-Est2p-Tlc1 complex was partially purified by ammonium sulphate fractionation and affinity chromatography on glutathione beads, and the partially purified telomerase did not contain the other two subunits of the telomerase holoenzyme, Est1p and Est3p. Ammonium Sulfate 53-70 TLC1 Saccharomyces cerevisiae S288C 14-18 15813705-4 2005 The GST-Est2p-Tlc1 complex was partially purified by ammonium sulphate fractionation and affinity chromatography on glutathione beads, and the partially purified telomerase did not contain the other two subunits of the telomerase holoenzyme, Est1p and Est3p. Glutathione 116-127 TLC1 Saccharomyces cerevisiae S288C 14-18 12167699-2 2002 The RNA component of yeast telomerase (Tlc1) is synthesized as a polyadenylated precursor and then processed to a mature poly(A)- form. Poly A 121-128 TLC1 Saccharomyces cerevisiae S288C 39-43 15531893-4 2004 The effects of Ku on telomerase binding require a 48-nucleotide (nt) stem-loop region of TLC1 telomerase RNA. 48-nucleotide 50-63 TLC1 Saccharomyces cerevisiae S288C 89-93 12167699-9 2002 Second, Mtr10p may be necessary for the nuclear import of some enzyme needed for the nuclear processing and maturation of Tlc1, and in the absence of this maturation, poly(A)+ Tlc1 is aberrantly exported to the cytoplasm (the "processing enzyme" model). Poly A 167-174 TLC1 Saccharomyces cerevisiae S288C 122-126 12167699-9 2002 Second, Mtr10p may be necessary for the nuclear import of some enzyme needed for the nuclear processing and maturation of Tlc1, and in the absence of this maturation, poly(A)+ Tlc1 is aberrantly exported to the cytoplasm (the "processing enzyme" model). Poly A 167-174 TLC1 Saccharomyces cerevisiae S288C 176-180 8610124-7 1996 The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Phosphorus-32 72-75 TLC1 Saccharomyces cerevisiae S288C 37-43 10733598-5 2000 Previously, we showed that a specific trinucleotide substitution in the Saccharomyces cerevisiae telomerase gene (TLC1) RNA template abolished the enzymatic activity of telomerase, causing the same cell senescence and telomere shortening phenotypes as a complete tlc1 deletion. trinucleotide 38-51 TLC1 Saccharomyces cerevisiae S288C 114-118 10733598-5 2000 Previously, we showed that a specific trinucleotide substitution in the Saccharomyces cerevisiae telomerase gene (TLC1) RNA template abolished the enzymatic activity of telomerase, causing the same cell senescence and telomere shortening phenotypes as a complete tlc1 deletion. trinucleotide 38-51 TLC1 Saccharomyces cerevisiae S288C 263-267 9042865-4 1997 We mutated the S. cerevisiae telomerase RNA (TLC1) with a series of 3-base (GUG) substitutions in and next to the 17-nucleotide templating domain. 17-nucleotide 114-127 TLC1 Saccharomyces cerevisiae S288C 45-49 8610124-7 1996 The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Phosphorus-32 72-75 TLC1 Saccharomyces cerevisiae S288C 37-41 8610124-7 1996 The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. 2'-deoxycytidine 5'-triphosphate 84-88 TLC1 Saccharomyces cerevisiae S288C 37-43 8610124-7 1996 The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. 2'-deoxycytidine 5'-triphosphate 84-88 TLC1 Saccharomyces cerevisiae S288C 37-41