ArticleArchives of biochemistry and biophysics2010
Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae.
Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- Life beyond 6000 genes: from sequence to synthesis in a post-genomics era.FEMS yeast research · 2026Review
- METTL10-Mediated PIAS3 Methylation Links Purine Metabolism to Gastric Cancer Progression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Misregulation of cell cycle-dependent methylation of budding yeast CENP-A contributes to chromosomal instability.Molecular biology of the cell · 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
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.Nucleic acids research · 2020Article
- Using Yeast to Define the Regulatory Role of Protein Lysine Methylation.Current protein & peptide science · 2020Review
- Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase.The Journal of biological chemistry · 2019Article
- Evolutionary insights into Trm112-methyltransferase holoenzymes involved in translation between archaea and eukaryotes.Nucleic acids research · 2018Article
- Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Regulation of eukaryotic elongation factor 1 alpha (eEF1A) by dynamic lysine methylation.RNA biology · 2018Article
- METTL21B Is a Novel Human Lysine Methyltransferase of Translation Elongation Factor 1A: Discovery by CRISPR/Cas9 Knockout.Molecular & cellular proteomics : MCP · 2017Article
- Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation.Nucleic acids research · 2017Article
- Human METTL12 is a mitochondrial methyltransferase that modifies citrate synthase.FEBS letters · 2017Article
- The novel lysine specific methyltransferase METTL21B affects mRNA translation through inducible and dynamic methylation of Lys-165 in human eukaryotic elongation factor 1 alpha (eEF1A).Nucleic acids research · 2017Article
- Ribosomal protein methyltransferases in the yeast Saccharomyces cerevisiae: Roles in ribosome biogenesis and translation.Biochemical and biophysical research communications · 2016Article
- Novel N-terminal and Lysine Methyltransferases That Target Translation Elongation Factor 1A in Yeast and Human.Molecular & cellular proteomics : MCP · 2016Article
- Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase.PloS one · 2015Article
- A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.Biochemical and biophysical research communications · 2014Article
- An unexpected journey: lysine methylation across the proteome.Biochimica et biophysica acta · 2014Review
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Authors and funding
3 authors.
Funding
Abstract
Eukaryotic elongation factor 1A (eEF1A) is an abundant cytosolic protein in Saccharomyces cerevisiae and is well conserved amongst species. This protein undergoes multiple posttranslational modifications, including the N-methylation of four side chain lysine residues. However, the enzyme(s) responsible for catalyzing these modifications have remained elusive. Here we show by intact protein mass spectrometry that deletion of either of two genes coding for putative methyltransferases results in a loss in mass of eEF1A. Deletion of the YHL039W gene, a member of the SET domain subfamily including cytochrome c and ribosomal protein lysine methyltransferases, results in an eEF1A mass loss corresponding to a single methyl group. Deletion in the YIL064W/SEE1 gene, encoding a well conserved seven beta strand methyltransferase sequence, has been shown previously to affect vesicle transport; in this work we show that deletion results in the loss of two methyl group equivalents from eEF1A. We find that deletion of thirty-five other putative and established SET domain and seven beta strand methyltransferases has no effect on the mass of eEF1A. Finally, we show that wild type extracts, but not YIL064W/SEE1 mutant extracts, can catalyze the S-adenosylmethionine-dependent in vitro methylation of hypomethylated eEF1A. We suggest that YHL039W (now designated EFM1 for elongation factor methyltransferase 1) and YIL064W/SEE1 encode distinct eEF1A methyltransferases that respectively monomethylate and dimethylate this protein at lysine residues.
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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 Socratic graph.