Evidence map›Paper›PMID 30715476›Full record

ArticleNucleic acids research2019

Characterization of a metazoan ADA acetyltransferase complex.

Jelly H M Soffers, Xuanying Li, Anita Saraf, Christopher W Seidel, Laurence Florens, Michael P Washburn, Susan M Abmayr, Jerry L Workman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structure of the human SAGA coactivator complex.Nature structural & molecular biology · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  12. Complex functions of Gcn5 and Pcaf in development and disease.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. 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

8 authors at 1 institution in 1 country.

Jelly H M SoffersStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Xuanying LiStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Anita SarafStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Christopher W SeidelStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Laurence FlorensStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Michael P WashburnStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Susan M AbmayrStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Jerry L WorkmanStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Stowers Institute for Medical Research · US

Funding

Transcription regulation in chromatinR35GM118068 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI JERRY L WORKMAN · 2016 to 2026
$4.2M
NIGMS NIH HHS R35 GM118068
6 · The paper itself

Abstract

The Gcn5 acetyltransferase functions in multiple acetyltransferase complexes in yeast and metazoans. Yeast Gcn5 is part of the large SAGA (Spt-Ada-Gcn5 acetyltransferase) complex and a smaller ADA acetyltransferase complex. In flies and mammals, Gcn5 (and its homolog pCAF) is part of various versions of the SAGA complex and another large acetyltransferase complex, ATAC (Ada2A containing acetyltransferase complex). However, a complex analogous to the small ADA complex in yeast has never been described in metazoans. Previous studies in Drosophila hinted at the existence of a small complex which contains Ada2b, a partner of Gcn5 in the SAGA complex. Here we have purified and characterized the composition of this complex and show that it is composed of Gcn5, Ada2b, Ada3 and Sgf29. Hence, we have named it the metazoan 'ADA complex'. We demonstrate that the fly ADA complex has histone acetylation activity on histones and nucleosome substrates. Moreover, ChIP-Sequencing experiments identified Ada2b peaks that overlap with another SAGA subunit, Spt3, as well as Ada2b peaks that do not overlap with Spt3 suggesting that the ADA complex binds chromosomal sites independent of the larger SAGA complex.

Indexed as

AnimalsCell LineChromatinDrosophila melanogasterDrosophila ProteinsHistone AcetyltransferasesMultienzyme ComplexesNuclear Proteinsp300-CBP-Associated FactorTrans-ActivatorsAda2a protein, DrosophilaADA3 protein, DrosophilaChromatinDrosophila ProteinsGCN5 protein, DrosophilaHistone AcetyltransferasesMultienzyme ComplexesNuclear Proteinsp300-CBP-Associated FactorSgf29 protein, DrosophilaTrans-Activators

Identifiers

PMID30715476
PMCPMC6468242
OpenAlexW2913638447

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.