ArticleNucleic acids research2003
Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 51 citations in OpenAlex.
- Exosome-mediated decay of unstable long extended precursors of human telomerase RNA is dependent on 5'-cap trimethylation.Genes & development · 2026Article
- Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy.Nucleic acids research · 2025Article
- Methylated guanosine and uridine modifications inRSC chemical biology · 2023Article
- PIMT Controls Insulin Synthesis and Secretion through PDX1.International journal of molecular sciences · 2023Article
- A Trimethylguanosine Synthase1-like (TGS1) homologue is implicated in vernalisation and flowering time control.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Article
- Identification and structural analysis of the Schizosaccharomyces pombe SMN complex.Nucleic acids research · 2021Article
- Loss of the RNA trimethylguanosine cap is compatible with nuclear accumulation of spliceosomal snRNAs but not pre-mRNA splicing or snRNA processing during animal development.PLoS genetics · 2020Article
- Intimate functional interactions between TGS1 and the Smn complex revealed by an analysis of the Drosophila eye development.PLoS genetics · 2020Article
- Loss of Human TGS1 Hypermethylase Promotes Increased Telomerase RNA and Telomere Elongation.Cell reports · 2020Article
- PIMT/NCOA6IP Deletion in the Mouse Heart Causes Delayed Cardiomyopathy Attributable to Perturbation in Energy Metabolism.International journal of molecular sciences · 2018Article
- The conserved AU dinucleotide at the 5' end of nascent U1 snRNA is optimized for the interaction with nuclear cap-binding-complex.Nucleic acids research · 2017Article
- Trimethylguanosine Synthase1 (TGS1) Is Essential for Chilling Tolerance.Plant physiology · 2017Article
- Self-association of Trimethylguanosine Synthase Tgs1 is required for efficient snRNA/snoRNA trimethylation and pre-rRNA processing.Scientific reports · 2015Article
- RNA methyltransferases involved in 5' cap biosynthesis.RNA biology · 2014Review
- Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome.PloS one · 2011Article
- Mapping the binding site of snurportin 1 on native U1 snRNP by cross-linking and mass spectrometry.Nucleic acids research · 2010Article
- Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis.Molecular cell · 2010Article
- Mutational analyses of trimethylguanosine synthase (Tgs1) and Mud2: proteins implicated in pre-mRNA splicing.RNA (New York, N.Y.) · 2010Article
- 5' and 3' end modifications of spliceosomal RNAs in Plasmodium falciparum.Molecular biology reports · 2010Article
- Cap analog substrates reveal three clades of cap guanine-N2 methyltransferases with distinct methyl acceptor specificities.RNA (New York, N.Y.) · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Saccharomyces cerevisiae Tgs1 methyltransferase (MTase) is responsible for conversion of the m(7)G caps of snRNAs and snoRNAs to a 2,2,7- trimethylguanosine structure. To learn more about the evolutionary origin of Tgs1 and to identify structural features required for its activity, we performed a structure-function study. By using sequence comparison and phylogenetic analysis, we found that Tgs1 shows strongest similarity to Mj0882, a protein related to a family comprised of bacterial rRNA:m(2)G MTases RsmC and RsmD. The structural information of Mj0882 was used to build a homology model of Tgs1p which allowed us to predict the range of the minimal globular MTase domain and the localization of other residues that may be important for enzyme function. To further characterize functional domains of Tgs1, mutants were constructed and tested for their effects on cell viability, subcellular localization and binding to the small nuclear ribonucleoproteins (snRNPs) and small nucleolar RNPs (snoRNPs). We found that the N-terminal domain of the hypermethylase is dispensable for binding to the common snRNPs and snoRNPs proteins but essential for correct nucleolar localization. Site- directed mutagenesis of Tgs1 allowed also the identification of the residues likely to be involved in the formation of the m7G-binding site and the catalytic center.
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