n(2)-n(2)-7-trimethylguanosine and 7-methylguanosine-triphosphate

n(2)-n(2)-7-trimethylguanosine has been researched along with 7-methylguanosine-triphosphate* in 1 studies

Other Studies

1 other study(ies) available for n(2)-n(2)-7-trimethylguanosine and 7-methylguanosine-triphosphate

Article	Year
Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Molecular cell, 2002, Volume: 9, Issue:4 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. Topics: Amino Acid Motifs; Autoantigens; Cell Nucleolus; Cold Temperature; Evolution, Molecular; Guanosine; Hydro-Lyases; Methylation; Methyltransferases; Microtubule-Associated Proteins; Nuclear Proteins; Phenotype; Protein Structure, Tertiary; Recombinant Fusion Proteins; Ribonucleoproteins, Small Nuclear; Ribonucleoproteins, Small Nucleolar; RNA Cap Analogs; RNA Caps; RNA Splicing; RNA-Binding Proteins; RNA, Fungal; RNA, Small Nuclear; RNA, Small Nucleolar; S-Adenosylmethionine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Two-Hybrid System Techniques	2002

Article

Year

Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus.

Molecular cell, 2002, Volume: 9, Issue:4

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.

Topics: Amino Acid Motifs; Autoantigens; Cell Nucleolus; Cold Temperature; Evolution, Molecular; Guanosine; Hydro-Lyases; Methylation; Methyltransferases; Microtubule-Associated Proteins; Nuclear Proteins; Phenotype; Protein Structure, Tertiary; Recombinant Fusion Proteins; Ribonucleoproteins, Small Nuclear; Ribonucleoproteins, Small Nucleolar; RNA Cap Analogs; RNA Caps; RNA Splicing; RNA-Binding Proteins; RNA, Fungal; RNA, Small Nuclear; RNA, Small Nucleolar; S-Adenosylmethionine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Two-Hybrid System Techniques

2002