ArticleRNA (New York, N.Y.)2003
In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p.
Article in RNA (New York, N.Y.), 2003. 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, 48 citations in OpenAlex.
- Article
- The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Proteomic analyses reveal new features of the box H/ACA RNP biogenesis.Nucleic acids research · 2023Article
- Article
- Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018Article
- Article
- Histone methylation modifiers in cellular signaling pathways.Cellular and molecular life sciences : CMLS · 2015Review
- Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum.Parasitology research · 2014Article
- Interactions affected by arginine methylation in the yeast protein-protein interaction network.Molecular & cellular proteomics : MCP · 2013Article
- Genomic insights of protein arginine methyltransferase Hmt1 binding reveals novel regulatory functions.BMC genomics · 2012Article
- Article
- Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications.BMC genomics · 2010Article
- Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2010Article
- Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Nucleic acids research · 2009Article
- Characterization of PRMT1 from Plasmodium falciparum.The Biochemical journal · 2009Article
- Functional connection between histone acetyltransferase Gcn5p and methyltransferase Hmt1p.Biochimica et biophysica acta · 2009Article
- Protein modifications in transcription elongation.Biochimica et biophysica acta · 2009Review
- Snu56p is required for Mer1p-activated meiotic splicing.Molecular and cellular biology · 2008Article
- Protein arginine methyltransferases: from unicellular eukaryotes to humans.Eukaryotic cell · 2007Review
- Unusual features of fibrillarin cDNA and gene structure in Euglena gracilis: evolutionary conservation of core proteins and structural predictions for methylation-guide box C/D snoRNPs throughout the domain Eucarya.Nucleic acids research · 2005Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In this report, we have investigated the impact of arginine methylation on the Gar1, Nop1, and Nsr1 nucleolar proteins in Saccharomyces cerevisiae. Although previous reports have established that protein arginine methylation is important for nucleocytoplasmic shuttling, they have focused on the examination of heterogeneous nuclear ribonucleoproteins (hnRNPs). We have extended this analysis to several nucleolar proteins that represent a distinct functional class of arginine-methylated proteins. We first developed an in vivo assay to identify proteins methylated by the Hmt1 arginine methyltransferase. This assay is based on the fact that the Hmt1 enzyme utilizes S-Adenosyl-L-methionine as the methyl donor for protein arginine methylation. Following SDS polyacrylamide electrophoresis, 11 distinct proteins were identified as substrates for the Hmt1 methyltransferase. Hmt1p overexpression did not increase the methylation level on these proteins, suggesting they are fully methylated under the conditions examined. Three of the radiolabeled proteins were confirmed to be Gar1p, Nop1p, and Nsr1p. To monitor the cellular localization of these proteins, functional GFP fusion proteins were generated and found to be localized to the nucleolus. This localization was independent of arginine methylation. Furthermore, all three proteins examined did not export to the cytoplasm. In contrast, arginine methylation is required for the export of the nuclear RNA-binding proteins Npl3p, Hrp1p, and Nab2p. The observation that three nucleolar proteins are modified by Hmt1p but are not exported from the nucleolus implies an alternate role for arginine methylation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.