title: Translational roles of elongation factor 2 protein lysine methylation.
abstract: Methylation of various components of the translational machinery has been shown to globally affect protein synthesis. Little is currently known about the role of lysine methylation on elongation factors. Here we show that in Saccharomyces cerevisiae, the product of the EFM3/YJR129C gene is responsible for the trimethylation of lysine 509 on elongation factor 2. Deletion of EFM3 or of the previously described EFM2 increases sensitivity to antibiotics that target translation and decreases translational fidelity. Furthermore, the amino acid sequences of Efm3 and Efm2, as well as their respective methylation sites on EF2, are conserved in other eukaryotes. These results suggest the importance of lysine methylation modification of EF2 in fine tuning the translational apparatus.
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
authors.forename: Maria C
authors.initials: MC
authors.lastname: Dzialo
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
authors.forename: Kyle J
authors.initials: KJ
authors.lastname: Travaglini
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
authors.forename: Sean
authors.initials: S
authors.lastname: Shen
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
authors.forename: Kevin
authors.initials: K
authors.lastname: Roy
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
authors.forename: Guillaume F
authors.initials: GF
authors.lastname: Chanfreau
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095; Department of Biological Chemistry and UCLA/Department of Energy Institute for Genomics and Proteomics, UCLA, Los Angeles, California 90095.
authors.forename: Joseph A
authors.initials: JA
authors.lastname: Loo
authors.affiliation: Department of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095. Electronic address: clarke@chem.ucla.edu.
authors.forename: Steven G
authors.initials: SG
authors.lastname: Clarke
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020652:Peptide Elongation Factor 2 / Q000378:metabolism*; D010802:Phylogeny; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000502:physiology*
chemical_list: D020652:Peptide Elongation Factor 2; D029701:Saccharomyces cerevisiae Proteins; C000594046:Efm2 protein, S cerevisiae; D008780:Methyltransferases; C523514:YJR129C protein, S cerevisiae
keywords: Lysine Methylation; Protein Methylation; Protein Synthesis; Ribosome Function; S-Adenosylmethionine (SAM); Translation Elongation Factor