Evidence map›Paper›PMID 11731478›Full record

ArticleGenes & development2001

Histone H3 specific acetyltransferases are essential for cell cycle progression.

L Howe, D Auston, P Grant, S John, R G Cook, J L Workman, L Pillus

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
–field-weighted citation impact
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

118 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
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  6. Frontiers in epigenetics and epigenomics · 2024
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  15. Article
  16. Do Epigenetic Timers Control Petal Development?Frontiers in plant science · 2021
    Review
  17. Article
  18. Review
  19. Article
  20. Review

58 more citing papers are in PubMed but not listed here.

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 4 institutions in 1 country.

L HoweHoward Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
D Auston
P Grant
S John
R G Cook
J L Workman
L Pillus
Pennsylvania State University · USHoward Hughes Medical Institute · USBaylor College of Medicine · USUniversity of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Longstanding observations suggest that acetylation and/or amino-terminal tail structure of histones H3 and H4 are critical for eukaryotic cells. For Saccharomyces cerevisiae, loss of a single H4-specific histone acetyltransferase (HAT), Esa1p, results in cell cycle defects and death. In contrast, although several yeast HAT complexes preferentially acetylate histone H3, the catalytic subunits of these complexes are not essential for viability. To resolve the apparent paradox between the significance of H3 versus H4 acetylation, we tested the hypothesis that H3 modification is essential, but is accomplished through combined activities of two enzymes. We observed that Sas3p and Gcn5p HAT complexes have overlapping patterns of acetylation. Simultaneous disruption of SAS3, the homolog of the MOZ leukemia gene, and GCN5, the hGCN5/PCAF homolog, is synthetically lethal due to loss of acetyltransferase activity. This key combination of activities is specific for these two HATs because neither is synthetically lethal with mutations of other MYST family or H3-specific acetyltransferases. Further, the combined loss of GCN5 and SAS3 functions results in an extensive, global loss of H3 acetylation and arrest in the G(2)/M phase of the cell cycle. The strikingly similar effect of loss of combined essential H3 HAT activities and the loss of a single essential H4 HAT underscores the fundamental biological significance of each of these chromatin-modifying activities.

Indexed as

Cell CycleDNA-Binding ProteinsSaccharomyces cerevisiaeAcetylationAcetyltransferasesBlotting, WesternCatalysisCrosses, GeneticFlow CytometryFungal ProteinsGenes, EssentialGenes, LethalHistone AcetyltransferasesHistonesMacromolecular Substancesp300-CBP-Associated FactorAcetyltransferasesADA2 protein, S cerevisiaeDNA-Binding ProteinsFungal ProteinsGCN5 protein, S cerevisiaeHistone AcetyltransferasesHistonesMacromolecular Substancesp300-CBP-Associated FactorProtein KinasesSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID11731478
PMCPMC312843
OpenAlexW2162865374

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.