Evidence map›Paper›PMID 18493053›Full record

ArticleGenetics2008

Regulators of cellular levels of histone acetylation in Saccharomyces cerevisiae.

Weimin Peng, Cynthia Togawa, Kangling Zhang, Siavash K Kurdistani

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Lysine acetylation regulates the activity of nuclear Pif1.The Journal of biological chemistry · 2020
    Article
  5. Review
  6. Article
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  15. Article
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  17. Drosophila models of cardiac disease.Progress in molecular biology and translational science · 2011
    Review
  18. Article
  19. Review
  20. Chemical induction of silent biosynthetic pathway transcription in Aspergillus niger.Journal of industrial microbiology & biotechnology · 2009
    Article
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

4 authors at 2 institutions in 1 country.

Weimin PengDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
Cynthia Togawa
Kangling Zhang
Siavash K Kurdistani
University of California, Los Angeles · USLoma Linda University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone acetylation levels are regulated through the opposing activities of histone acetyltransferases (HATs) and deacetylases (HDACs). While much is known about gene-specific control of histone acetylation, little is understood about how total or cellular levels of histone acetylation are regulated. To identify regulators of cellular levels of histone acetylation, we developed an immunofluorescence-based approach to screen the single-gene deletion library of Saccharomyces cerevisiae for strains with significant reductions in cellular histone acetylation levels. Of the 4848 mutants screened, we identified 63 strains with considerable cellular hypoacetylation of N-terminal lysines in histones H3 and H4. The cellular hypoacetylation was validated for subsets of the identified strains through secondary screens including mass spectrometric analysis of individual lysines and chromatin immunoprecipitation of specific genomic loci. Among the identified mutants were several members of the Ccr4-Not complex, V-type ATPases, and vacuolar protein-sorting complexes as well as genes with unknown functions. We show that Gcn5, a major HAT in yeast, has diminished histone acetyltransferase activity in particular mutants, providing a plausible explanation for reduction of cellular acetylation levels in vivo. Our findings have revealed unexpected and novel links between histone acetylation, Gcn5 HAT activity, and diverse processes such as transcription, cellular ion homeostasis, and protein transport.

Indexed as

AcetylationBlotting, WesternChromatin ImmunoprecipitationFluorescent Antibody TechniqueGenomicsHistone AcetyltransferasesHistonesMass SpectrometryMutationSaccharomyces cerevisiaeHistone AcetyltransferasesHistones

Identifiers

PMID18493053
PMCPMC2390606
OpenAlexW2133035149

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.