Document Detail


Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus.
MedLine Citation:
PMID:  11983179     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The m(7)G caps of most spliceosomal snRNAs and certain snoRNAs are converted posttranscriptionally to 2,2,7-trimethylguanosine (m(3)G) cap structures. Here, we show that yeast Tgs1p, an evolutionarily conserved protein carrying a signature of S-AdoMet methyltransferase, is essential for hypermethylation of the m(7)G caps of both snRNAs and snoRNAs. Deletion of the yeast TGS1 gene abolishes the conversion of the m(7)G to m(3)G caps and produces a cold-sensitive splicing defect that correlates with the retention of U1 snRNA in the nucleolus. Consistently, Tgs1p is also localized in the nucleolus. Our results suggest a trafficking pathway in which yeast snRNAs and snoRNAs cycle through the nucleolus to undergo m(7)G cap hypermethylation.
Authors:
John Mouaikel; Céline Verheggen; Edouard Bertrand; Jamal Tazi; Rémy Bordonné
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular cell     Volume:  9     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-05-01     Completed Date:  2002-06-14     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  891-901     Citation Subset:  IM    
Affiliation:
Institut de Génétique Moléculaire, IFR 24-CNRS UMR 5535, 1919 route de Mende, 34000 Montpellier, France.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Autoantigens / physiology
Cell Nucleolus / enzymology*
Cold Temperature
Evolution, Molecular
Guanosine / analogs & derivatives,  metabolism*
Hydro-Lyases*
Methylation
Methyltransferases / genetics,  physiology*
Microtubule-Associated Proteins / metabolism
Nuclear Proteins / metabolism
Phenotype
Protein Structure, Tertiary
RNA Cap Analogs / biosynthesis*,  physiology
RNA Caps / metabolism*
RNA Splicing / genetics
RNA, Fungal / metabolism*
RNA, Small Nuclear / metabolism*
RNA, Small Nucleolar / metabolism*
RNA-Binding Proteins / metabolism
Recombinant Fusion Proteins / metabolism
Ribonucleoproteins, Small Nuclear / physiology
Ribonucleoproteins, Small Nucleolar*
S-Adenosylmethionine / metabolism
Saccharomyces cerevisiae / enzymology,  genetics*
Saccharomyces cerevisiae Proteins / genetics,  physiology*
Sequence Homology, Amino Acid
Substrate Specificity
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Autoantigens; 0/Microtubule-Associated Proteins; 0/NOP58 protein, S cerevisiae; 0/Nuclear Proteins; 0/RNA Cap Analogs; 0/RNA Caps; 0/RNA, Fungal; 0/RNA, Small Nuclear; 0/RNA, Small Nucleolar; 0/RNA-Binding Proteins; 0/Recombinant Fusion Proteins; 0/Ribonucleoproteins, Small Nuclear; 0/Ribonucleoproteins, Small Nucleolar; 0/SMB protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/U1 small nuclear RNA; 118-00-3/Guanosine; 26554-26-7/7-methylguanosine triphosphate; 29908-03-0/S-Adenosylmethionine; 40027-70-1/N(2),N(2),7-trimethylguanosine; EC 2.1.1.-/Methyltransferases; EC 2.1.1.-/trimethylguanosine synthase; EC 4.2.1.-/Hydro-Lyases; EC 4.2.1.70/CBF5 protein, S cerevisiae

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