Evidence map›Paper›PMID 21460220›Full record

ArticleThe Journal of biological chemistry2011

The ribosomal l1 protuberance in yeast is methylated on a lysine residue catalyzed by a seven-beta-strand methyltransferase.

Kristofor J Webb, Qais Al-Hadid, Cecilia I Zurita-Lopez, Brian D Young, Rebecca S Lipson, Steven G Clarke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. 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
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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

6 authors at 1 institution in 1 country.

Kristofor J WebbDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, California 90095-1569, USA.
Qais Al-Hadid
Cecilia I Zurita-Lopez
Brian D Young
Rebecca S Lipson
Steven G Clarke
University of California, Los Angeles · US

Funding

CONTROL OF EUCARYOTIC FUNCTION BY METHYLATIONR37GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2009
$5.0M
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 GM026020NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R37 GM026020
6 · The paper itself

Abstract

Modification of proteins of the translational apparatus is common in many organisms. In the yeast Saccharomyces cerevisiae, we provide evidence for the methylation of Rpl1ab, a well conserved protein forming the ribosomal L1 protuberance of the large subunit that functions in the release of tRNA from the exit site. We show that the intact mass of Rpl1ab is 14 Da larger than its calculated mass with the previously described loss of the initiator methionine residue and N-terminal acetylation. We determined that the increase in mass of yeast Rpl1ab is consistent with the addition of a methyl group to lysine 46 using top-down mass spectrometry. Lysine modification was confirmed by detecting (3)H-N-ε-monomethyllysine in hydrolysates of Rpl1ab purified from yeast cells radiolabeled in vivo with S-adenosyl-l-[methyl-(3)H]methionine. Mass spectrometric analysis of intact Rpl1ab purified from 37 deletion strains of known and putative yeast methyltransferases revealed that only the deletion of the YLR137W gene, encoding a seven-β-strand methyltransferase, results in the loss of the +14-Da modification. We expressed the YLR137W gene as a His-tagged protein in Escherichia coli and showed that it catalyzes N-ε-monomethyllysine formation within Rpl1ab on ribosomes from the ΔYLR137W mutant strain lacking the methyltransferase activity but not from wild-type ribosomes. We also showed that the His-tagged protein could catalyze monomethyllysine formation on a 16-residue peptide corresponding to residues 38-53 of Rpl1ab. We propose that the YLR137W gene be given the standard name RKM5 (ribosomal lysine (K) methyltransferase 5). Orthologs of RKM5 are found only in fungal species, suggesting a role unique to their survival.

Indexed as

Escherichia coliMass SpectrometryMethylationMutationProtein MethyltransferasesRecombinant ProteinsRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein MethyltransferasesRecombinant ProteinsRibosomal ProteinsRPL1A protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID21460220
PMCPMC3099657
OpenAlexW1977919788

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.