Evidence map›Paper›PMID 20864530›Full record

ArticleThe Journal of biological chemistry2010

A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is dependent upon the YIL110W methyltransferase.

Kristofor J Webb, Cecilia I Zurita-Lopez, Qais Al-Hadid, Arthur Laganowsky, Brian D Young, Rebecca S Lipson, Puneet Souda, Kym F Faull, Julian P Whitelegge, Steven G Clarke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

55 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. METTL18 is Required for Developmental, Metabolic, and Endocrine Regulation of Mammalian Growth.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Substrate selectivity of human histidine methyltransferase METTL9.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Review
  6. Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. Article
  15. Article
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  19. Article
  20. Review
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

10 authors at 1 institution in 1 country.

Kristofor J WebbDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90095-1569, USA.
Cecilia I Zurita-Lopez
Qais Al-Hadid
Arthur Laganowsky
Brian D Young
Rebecca S Lipson
Puneet Souda
Kym F Faull
Julian P Whitelegge
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

We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-(3)H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using high-resolution cation-exchange chromatography and thin layer chromatography, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhistidine residue is present. Analysis of 37 deletion strains of known and putative methyltransferases revealed that only the deletion of the YIL110W gene, encoding a seven β-strand methyltransferase, results in the loss of the +14-Da modification of Rpl3. We suggest that YIL110W encodes a protein histidine methyltransferase responsible for the modification of Rpl3 and potentially other yeast proteins, and now designate it Hpm1 (Histidine protein methyltransferase 1). Deletion of the YIL110W/HPM1 gene results in numerous phenotypes including some that may result from abnormal interactions between Rpl3 and the 25 S ribosomal RNA. This is the first report of a methylated histidine residue in yeast cells, and the first example of a gene required for protein histidine methylation in nature.

Indexed as

Amino Acid SequenceMethylhistidinesMethyltransferasesMolecular Sequence DataRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Alignment3-methylhistidineHpm1 protein, S cerevisiaeMethylhistidinesMethyltransferasesRibosomal ProteinsRpl3 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID20864530
PMCPMC2988365
OpenAlexW2051056168

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Registered trials

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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 OpenQuestion graph.