ArticleBiochemistry2012
Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
- The N-terminal extension of ribosomal protein Rps2 shapes its early fate through Chaperone-Importin competition and arginine methylation.The Journal of biological chemistry · 2026Article
- Therapeutic Targeting of Protein Lysine and Arginine Methyltransferases: Principles and Strategies for Inhibitor Design.International journal of molecular sciences · 2025Review
- Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024Review
- Misregulation of cell cycle-dependent methylation of budding yeast CENP-A contributes to chromosomal instability.Molecular biology of the cell · 2023Article
- Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5).Biomolecules · 2023Article
- 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
- Methylarginine efflux in nutrient-deprived yeast mitigates disruption of nitric oxide synthesis.Amino acids · 2023Article
- TheRNA (New York, N.Y.) · 2022Article
- The CAR-mRNA Interaction Surface Is a Zipper Extension of the Ribosome A Site.International journal of molecular sciences · 2022Article
- Global analysis of protein arginine methylation.Cell reports methods · 2021Article
- Methylation multiplicity and its clinical values in cancer.Expert reviews in molecular medicine · 2021Review
- Arginine Methylation Regulates Ribosome CAR Function.International journal of molecular sciences · 2021Article
- A Ribosome Interaction Surface Sensitive to mRNA GCN Periodicity.Biomolecules · 2020Article
- GCN sensitive protein translation in yeast.PloS one · 2020Article
- Tsr4 Is a Cytoplasmic Chaperone for the Ribosomal Protein Rps2 in Saccharomyces cerevisiae.Molecular and cellular biology · 2019Article
- How an ancient, salt-tolerant fruit crop, Ficus carica L., copes with salinity: a transcriptome analysis.Scientific reports · 2019Article
- A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.Biochemistry · 2019Article
- Structural and biochemical analysis of the dual-specificity Trm10 enzyme fromRNA (New York, N.Y.) · 2018Article
- The ribosome: A hot spot for the identification of new types of protein methyltransferases.The Journal of biological chemistry · 2018Article
- Dissecting ribosomal particles throughout the kingdoms of life using advanced hybrid mass spectrometry methods.Nature communications · 2018Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We have characterized the posttranslational methylation of Rps2, Rps3, and Rps27a, three small ribosomal subunit proteins in the yeast Saccharomyces cerevisiae, using mass spectrometry and amino acid analysis. We found that Rps2 is substoichiometrically modified at arginine-10 by the Rmt1 methyltransferase. We demonstrated that Rps3 is stoichiometrically modified by ω-monomethylation at arginine-146 by mass spectrometric and site-directed mutagenic analyses. Substitution of alanine for arginine at position 146 is associated with slow cell growth, suggesting that the amino acid identity at this site may influence ribosomal function and/or biogenesis. Analysis of the three-dimensional structure of Rps3 in S. cerevisiae shows that arginine-146 makes contacts with the small subunit rRNA. Screening of deletion mutants encoding potential yeast methyltransferases revealed that the loss of the YOR021C gene results in the absence of methylation of Rps3. We demonstrated that recombinant Yor021c catalyzes ω-monomethylarginine formation when incubated with S-adenosylmethionine and hypomethylated ribosomes prepared from a YOR021C deletion strain. Interestingly, Yor021c belongs to the family of SPOUT methyltransferases that, to date, have only been shown to modify RNA substrates. Our findings suggest a wider role for SPOUT methyltransferases in nature. Finally, we have demonstrated the presence of a stoichiometrically methylated cysteine residue at position 39 of Rps27a in a zinc-cysteine cluster. The discovery of these three novel sites of protein modification within the small ribosomal subunit will now allow for an analysis of their functional roles in translation and possibly other cellular processes.
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