Evidence map›Paper›PMID 32890768›Full record

ReviewBiochimica et biophysica acta. Gene regulatory mechanisms2021

The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.

Jose M Espinola-Lopez, Song Tan

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Gene regulatory mechanisms, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Genome-Wide Identification of Histone Acetyltransferases inJournal of fungi (Basel, Switzerland) · 2026
    Article
  7. Review
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  11. Review
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  17. Genome-Scale Screening ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  18. Article
  19. Article
  20. Frontiers in microbiology · 2024
    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

2 authors at 1 institution in 1 country.

Jose M Espinola-LopezCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Song TanCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address: stx30@psu.edu.
Pennsylvania State University · US

Funding

Structural studies of chromatin complexesR35GM127034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI SONG TAN · 2018 to 2026
$4.8M
Eukaryotic Gene Regulation (EGR) Predoctoral Training ProgramT32GM125592 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI REESE, JOSEPH C · 2018 to 2022
$920k
NIGMS NIH HHS R35 GM127034NIGMS NIH HHS T32 GM125592
6 · The paper itself

Abstract

Histone post-translational modifications are essential for the regulation of gene expression in eukaryotes. Gcn5 (KAT2A) is a histone acetyltransferase that catalyzes the post-translational modification at multiple positions of histone H3 through the transfer of acetyl groups to the free amino group of lysine residues. Gcn5 catalyzes histone acetylation in the context of a HAT module containing the Ada2, Ada3 and Sgf29 subunits of the parent megadalton SAGA transcriptional coactivator complex. Biochemical and structural studies have elucidated mechanisms for Gcn5's acetyl- and other acyltransferase activities on histone substrates, for histone H3 phosphorylation and histone H3 methylation crosstalks with histone H3 acetylation, and for how Ada2 increases Gcn5's histone acetyltransferase activity. Other studies have identified Ada2 isoforms in SAGA-related complexes and characterized variant Gcn5 HAT modules containing these Ada2 isoforms. In this review, we highlight biochemical and structural studies of Gcn5 and its functional interactions with Ada2, Ada3 and Sgf29.

Indexed as

Protein Processing, Post-TranslationalAcetylationCryoelectron MicroscopyHistone AcetyltransferasesHistonesIsoenzymesMethylationMultienzyme Complexesp300-CBP-Associated Factorp300-CBP Transcription FactorsPhosphorylationSaccharomyces cerevisiae ProteinsTranscription FactorsADA2 protein, S cerevisiaeGCN5 protein, S cerevisiaeHistone AcetyltransferasesHistonesIsoenzymesMultienzyme ComplexesNGG1 protein, S cerevisiaep300-CBP-Associated Factorp300-CBP Transcription FactorsSaccharomyces cerevisiae ProteinsSgf29 protein, S cerevisiaetGCN5 histone acetyltransferaseTranscription FactorsEpigenetic modificationGene regulationHistone crosstalksHistone modificationProtein isoformsTranscriptional regulation

Identifiers

PMID32890768
PMCPMC8351874
OpenAlexW3081864250

What OpenQuestion holds

Textmetadata
LicenceTDM
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.