Evidence map›Paper›PMID 23973296›Full record

ArticleCurrent biology : CB2013

Gcn5 and sirtuins regulate acetylation of the ribosomal protein transcription factor Ifh1.

Michael Downey, Britta Knight, Ajay A Vashisht, Charles A Seller, James A Wohlschlegel, David Shore, David P Toczyski

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  6. TheAging · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Yeast Crf1p: An activator in need is an activator indeed.Computational and structural biotechnology journal · 2022
    Review
  11. Review
  12. Review
  13. Article
  14. NADBiomolecules · 2020
    Review
  15. Article
  16. 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 3 institutions in 2 countries.

Michael DowneyDepartment of Biochemistry and Biophysics, Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, 1450 3(rd) Street, San Francisco, CA 94158, USA.
Britta Knight
Ajay A Vashisht
Charles A Seller
James A Wohlschlegel
David Shore
David P Toczyski
University of California, San Francisco · USUniversity of California, Los Angeles · USUniversity of Geneva · CH

Funding

Regulation and Targets of the DNA Damage CheckpointR01GM059691 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI TOCZYSKI, DAVID PAUL · 1999 to 2015
$5.8M
Proteolytic Control of Iron Metabolism by the Ubiquitin Ligase FBXL5R01GM089778 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WOHLSCHLEGEL, JAMES AKIRA · 2010 to 2023
$4.0M
NIGMS NIH HHS GM059691NIGMS NIH HHS GM89778NIGMS NIH HHS R01 GM059691NIGMS NIH HHS R01 GM089778
6 · The paper itself

Abstract

backgroundIn eukaryotes, ribosome biosynthesis involves the coordination of ribosomal RNA and ribosomal protein (RP) production. In S. cerevisiae, the regulation of ribosome biosynthesis occurs largely at the level of transcription. The transcription factor Ifh1 binds at RP genes and promotes their transcription when growth conditions are favorable. Although Ifh1 recruitment to RP genes has been characterized, little is known about the regulation of promoter-bound Ifh1.

resultsWe used a novel whole-cell-extract screening approach to identify Spt7, a member of the SAGA transcription complex, and the RP transactivator Ifh1 as highly acetylated nonhistone species. We report that Ifh1 is modified by acetylation specifically in an N-terminal domain. These acetylations require the Gcn5 histone acetyltransferase and are reversed by the sirtuin deacetylases Hst1 and Sir2. Ifh1 acetylation is regulated by rapamycin treatment and stress and limits the ability of Ifh1 to act as a transactivator at RP genes.

conclusionsOur data suggest a novel mechanism of regulation whereby Gcn5 functions to titrate the activity of Ifh1 following its recruitment to RP promoters to provide more than an all-or-nothing mode of transcriptional regulation. We provide insights into how the action of histone acetylation machineries converges with nutrient-sensing pathways to regulate important aspects of cell growth.

Indexed as

AcetylationHistone Acetyltransferasesp300-CBP-Associated FactorRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSirtuinsTrans-ActivatorsTranscription FactorsGCN5 protein, S cerevisiaeHistone AcetyltransferasesIFH1 protein, S cerevisiaep300-CBP-Associated FactorRibosomal ProteinsSaccharomyces cerevisiae ProteinsSirtuinsTrans-ActivatorsTranscription Factors

Identifiers

PMID23973296
PMCPMC3982851
OpenAlexW2161367297

What OpenQuestion holds

Textmetadata
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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.