Evidence map›Paper›PMID 24486316›Full record

ArticleBiochemical and biophysical research communications2014

Methylation of yeast ribosomal protein S2 is elevated during stationary phase growth conditions.

Daniel T Ladror, Brian L Frey, Mark Scalf, Mark E Levenstein, Jacklyn M Artymiuk, Lloyd M Smith

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Ribosome Specialization in Protozoa Parasites.International journal of molecular sciences · 2023
    Review
  3. Article
  4. 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

6 authors at 1 institution in 1 country.

Daniel T LadrorDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
Brian L FreyDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
Mark ScalfDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
Mark E LevensteinDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
Jacklyn M ArtymiukDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
Lloyd M SmithDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA. Electronic address: smith@chem.wisc.edu.
University of Wisconsin–Madison · US

Funding

Wisconsin Center of Excellence in Genomics ScienceP50HG004952 · NHGRI · TEXAS BIOMEDICAL RESEARCH INSTITUTE · PI OLIVIER, MICHAEL · 2009 to 2013
$13.0M
The Epigenotype of Human ES CellsP01GM081629 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI THOMSON, JAMES ALEXANDER · 2008 to 2012
$8.9M
NHGRI NIH HHS 1P50HG004952.NHGRI NIH HHS P50 HG004952NIGMS NIH HHS P01 GM081629NIGMS NIH HHS P01GM081629
6 · The paper itself

Abstract

Ribosomes, as the center of protein translation in the cell, require careful regulation via multiple pathways. While regulation of ribosomal synthesis and function has been widely studied on the transcriptional and translational "levels," the biological roles of ribosomal post-translational modifications (PTMs) are largely not understood. Here, we explore this matter by using quantitative mass spectrometry to compare the prevalence of ribosomal methylation and acetylation for yeast in the log phase and the stationary phase of growth. We find that of the 27 modified peptides identified, two peptides experience statistically significant changes in abundance: a 1.9-fold decrease in methylation for k(Me)VSGFKDEVLETV of ribosomal protein S1B (RPS1B), and a 10-fold increase in dimethylation for r(DiMe)GGFGGR of ribosomal protein S2 (RPS2). While the biological role of RPS1B methylation has largely been unexplored, RPS2 methylation is a modification known to have a role in processing and export of ribosomal RNA. This suggests that yeast in the stationary phase increase methylation of RPS2 in order to regulate ribosomal synthesis. These results demonstrate the utility of mass spectrometry for quantifying dynamic changes in ribosomal PTMs.

Indexed as

Amino Acid SequenceMethylationMolecular Sequence DataProtein Processing, Post-TranslationalRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsRibosomal Proteinsribosomal protein S2Saccharomyces cerevisiae ProteinsGrowth conditionsMass spectrometryPost-translational modificationsProteomicsRibosomeStationary phase

Identifiers

PMID24486316
PMCPMC3978127
OpenAlexW2083523651

What OpenQuestion holds

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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.