ArticleBiochemical and biophysical research communications2014
A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 18 citations in OpenAlex.
- 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
- Eukaryote-Conserved Methylarginine Is Absent in Diplomonads and Functionally Compensated in Giardia.Molecular biology and evolution · 2020Article
- Using Yeast to Define the Regulatory Role of Protein Lysine Methylation.Current protein & peptide science · 2020Review
- Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.Biochemistry · 2019Article
- 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
- 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
- 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
- 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The elongation factors of Saccharomyces cerevisiae are extensively methylated, containing a total of ten methyllysine residues. Elongation factor methyltransferases (Efm1, Efm2, Efm3, and Efm4) catalyze at least four of these modifications. Here we report the identification of a new type of protein lysine methyltransferase, Efm5 (Ygr001c), which was initially classified as N6-adenine DNA methyltransferase-like. Efm5 is required for trimethylation of Lys-79 on EF1A. We directly show the loss of this modification in efm5Δ strains by both mass spectrometry and amino acid analysis. Close homologs of Efm5 are found in vertebrates, invertebrates, and plants, although some fungal species apparently lack this enzyme. This suggests possible unique functions of this modification in S. cerevisiae and higher eukaryotes. The misannotation of Efm5 was due to the presence of a DPPF sequence in post-Motif II, typically associated with DNA methylation. Further analysis of this motif and others like it demonstrates a potential consensus sequence for N-methyltransferases.
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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.