ArticleMolecular and cellular biology2010
Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Npl3 is required for efficient autophagosome-vacuole fusion.Autophagy · 2026Article
- A Protein-Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20.International journal of molecular sciences · 2023Article
- Alternative splicing in neurodegenerative disease and the promise of RNA therapies.Nature reviews. Neuroscience · 2023Review
- Coordination of RNA Processing Regulation by Signal Transduction Pathways.Biomolecules · 2021Review
- Phylogenetic comparison and splice site conservation of eukaryotic U1 snRNP-specific U1-70K gene family.Scientific reports · 2021Article
- Dynamic mRNP Remodeling in Response to Internal and External Stimuli.Biomolecules · 2020Review
- Experimental evolution reveals a general role for the methyltransferase Hmt1 in noise buffering.PLoS biology · 2019Article
- Evolution of intron splicing towards optimized gene expression is based on various Cis- and Trans-molecular mechanisms.PLoS biology · 2019Article
- Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018Article
- Intron specificity in pre-mRNA splicing.Current genetics · 2018Review
- PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.Journal of biochemistry · 2017Article
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- Coupling and coordination in gene expression processes with pre-mRNA splicing.International journal of molecular sciences · 2015Review
- Interactions affected by arginine methylation in the yeast protein-protein interaction network.Molecular & cellular proteomics : MCP · 2013Article
- Review
- Genomic insights of protein arginine methyltransferase Hmt1 binding reveals novel regulatory functions.BMC genomics · 2012Article
- Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Intrinsic disorder in the human spliceosomal proteome.PLoS computational biology · 2012Article
- Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.PloS one · 2012Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cotranscriptional recruitment of pre-mRNA splicing factors to their genomic targets facilitates efficient and ordered assembly of a mature messenger ribonucleoprotein particle (mRNP). However, how the cotranscriptional recruitment of splicing factors is regulated remains largely unknown. Here, we demonstrate that protein arginine methylation plays a novel role in regulating this process in Saccharomyces cerevisiae. Our data show that Hmt1, the major type I arginine methyltransferase, methylates Snp1, a U1 small nuclear RNP (snRNP)-specific protein, and that the mammalian Snp1 homolog, U1-70K, is likewise arginine methylated. Genome-wide localization analysis reveals that the deletion of the HMT1 gene deregulates the recruitment of U1 snRNP and its associated components to intron-containing genes (ICGs). In the same context, splicing factors acting downstream of U1 snRNP addition bind to a reduced number of ICGs. Quantitative measurement of the abundance of spliced target transcripts shows that these changes in recruitment result in an increase in the splicing efficiency of developmentally regulated mRNAs. We also show that in the absence of either Hmt1 or of its catalytic activity, an association between Snp1 and the SR-like protein Npl3 is substantially increased. Together, these data support a model whereby arginine methylation modulates dynamic associations between SR-like protein and pre-mRNA splicing factor to promote target specificity in splicing.
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