Evidence map›Paper›PMID 25231983›Full record

ArticleThe Journal of biological chemistry2014

Translational roles of elongation factor 2 protein lysine methylation.

Maria C Dzialo, Kyle J Travaglini, Sean Shen, Kevin Roy, Guillaume F Chanfreau, Joseph A Loo, Steven G Clarke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. LC-MS profiling ofbioRxiv : the preprint server for biology · 2026
    Article
  2. 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 · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Maria C DzialoDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
Kyle J TravagliniDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
Sean ShenDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
Kevin RoyDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
Guillaume F ChanfreauDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095.
Joseph A LooDepartment 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.
Steven G ClarkeDepartment of Chemistry and Biochemistry and the Molecular Biology Institute and UCLA, Los Angeles, California 90095. Electronic address: clarke@chem.ucla.edu.
UCLA Health · USUCLA Medical Center · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
THE CONTROL OF GENE EXPRESSION BY EUKARYOTIC RNASE IIIR01GM061518 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHANFREAU, GUILLAUME F · 2000 to 2017
$5.5M
CONTROL OF EUCARYOTIC FUNCTION BY METHYLATIONR37GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2009
$5.0M
UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
CONTROL OF EUKARYOTIC MEMBRANE FUNCTION BY METHYLATIONR01GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 1985 to 2013
$2.1M
NIGMS NIH HHS GM007185NIGMS NIH HHS GM026020NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R01 GM061518NIGMS NIH HHS R01 GM103479NIGMS NIH HHS R37 GM026020NIGMS NIH HHS T32 GM007185
6 · The paper itself

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.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCatalytic DomainConserved SequenceMethylationMethyltransferasesModels, MolecularMolecular Sequence DataPeptide Elongation Factor 2PhylogenyProtein BiosynthesisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEfm2 protein, S cerevisiaeMethyltransferasesPeptide Elongation Factor 2Saccharomyces cerevisiae ProteinsYJR129C protein, S cerevisiaeLysine MethylationProtein MethylationProtein SynthesisRibosome FunctionS-Adenosylmethionine (SAM)Translation Elongation Factor

Identifiers

PMID25231983
PMCPMC4215232
OpenAlexW2085304602

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.