Evidence map›Paper›PMID 24865971›Full record

ArticleMolecular and cellular biology2014

Histidine methylation of yeast ribosomal protein Rpl3p is required for proper 60S subunit assembly.

Qais Al-Hadid, Kevin Roy, William Munroe, Maria C Dzialo, Guillaume F Chanfreau, Steven G Clarke

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Article
  6. Review
  7. Regulation of ribosomal protein genes: An ordered anarchy.Wiley interdisciplinary reviews. RNA · 2021
    Review
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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.

Qais Al-HadidDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA.
Kevin RoyDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA.
William MunroeDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA.
Maria C DzialoDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA.
Guillaume F ChanfreauDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA.
Steven G ClarkeDepartment of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California, USA clarke@mbi.ucla.edu.

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
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 GM061518NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R01 GM061518NIGMS NIH HHS R37 GM026020NIGMS NIH HHS T32 GM007185NIGMS NIH HHS T32GM007185
6 · The paper itself

Abstract

Histidine protein methylation is an unusual posttranslational modification. In the yeast Saccharomyces cerevisiae, the large ribosomal subunit protein Rpl3p is methylated at histidine 243, a residue that contacts the 25S rRNA near the P site. Rpl3p methylation is dependent upon the presence of Hpm1p, a candidate seven-beta-strand methyltransferase. In this study, we elucidated the biological activities of Hpm1p in vitro and in vivo. Amino acid analyses reveal that Hpm1p is responsible for all of the detectable protein histidine methylation in yeast. The modification is found on a polypeptide corresponding to the size of Rpl3p in ribosomes and in a nucleus-containing organelle fraction but was not detected in proteins of the ribosome-free cytosol fraction. In vitro assays demonstrate that Hpm1p has methyltransferase activity on ribosome-associated but not free Rpl3p, suggesting that its activity depends on interactions with ribosomal components. hpm1 null cells are defective in early rRNA processing, resulting in a deficiency of 60S subunits and translation initiation defects that are exacerbated in minimal medium. Cells lacking Hpm1p are resistant to cycloheximide and verrucarin A and have decreased translational fidelity. We propose that Hpm1p plays a role in the orchestration of the early assembly of the large ribosomal subunit and in faithful protein production.

Indexed as

Cell NucleusHistidineMethylationMethyltransferasesRibosomal ProteinsRibosomesRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistidineMethyltransferasesRibosomal ProteinsRNA PrecursorsRNA, RibosomalRNA, ribosomal, 25SSaccharomyces cerevisiae Proteins

Identifiers

PMID24865971
PMCPMC4135575
OpenAlexW2100444275

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.