Evidence map›Paper›PMID 24722339›Full record

ArticlePloS one2014

Histone deacetylase 1 and p300 can directly associate with chromatin and compete for binding in a mutually exclusive manner.

Xuehui Li, Hui Yang, Suming Huang, Yi Qiu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. BAP1 forms a trimer with HMGB1 and HDAC1 that modulates gene × environment interaction with asbestos.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Interactions and Feedbacks in E-Cadherin Transcriptional Regulation.Frontiers in cell and developmental biology · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Xuehui LiDepartment of Anatomy and Cell Biology, University of Florida, Gainesville, Florida, United States of America.
Hui YangDepartment of Anatomy and Cell Biology, University of Florida, Gainesville, Florida, United States of America.
Suming HuangDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida, United States of America.
Yi QiuDepartment of Anatomy and Cell Biology, University of Florida, Gainesville, Florida, United States of America.
University of Florida · US

Funding

Regulation of insulator function and globin gene expression by USF and associatedR01HL091929 · NHLBI · UNIVERSITY OF FLORIDA · PI HUANG, SUMING · 2009 to 2013
$2.0M
Transcriptional regulation of TAL1/SCL in normal and malignant hematopoiesisR01HL090589 · NHLBI · UNIVERSITY OF FLORIDA · PI HUANG, SUMING · 2008 to 2012
$1.9M
The role of HDAC1 acetylation on corepressor complex activity and hematopoiesisR01HL095674 · NHLBI · UNIVERSITY OF FLORIDA · PI QIU, YI · 2010 to 2013
$1.4M
NHLBI NIH HHS R01 HL 090589NHLBI NIH HHS R01 HL090589NHLBI NIH HHS R01 HL091929NHLBI NIH HHS R01 HL095674
6 · The paper itself

Abstract

Lysine acetyltransferases (KATs) and histone deacetylases (HDACs) are important epigenetic modifiers and dynamically cycled on active gene promoters to regulate transcription. Although HDACs are recruited to gene promoters and DNA hypersensitive sites through interactions with DNA binding factors, HDAC activities are also found globally in intergenic regions where DNA binding factors are not present. It is suggested that HDACs are recruited to those regions through other distinct, yet undefined mechanisms. Here we show that HDACs can be directly recruited to chromatin in the absence of other factors through direct interactions with both DNA and core histone subunits. HDACs interact with DNA in a non-sequence specific manner. HDAC1 and p300 directly bind to the overlapping regions of the histone H3 tail and compete for histone binding. Previously we show that p300 can acetylate HDAC1 to attenuate deacetylase activity. Here we have further mapped two distinct regions of HDAC1 that interact with p300. Interestingly, these regions of HDAC1 also associate with histone H3. More importantly, p300 and HDAC1 compete for chromatin binding both in vitro and in vivo. Therefore, the mutually exclusive associations of HDAC1/p300, p300/histone, and HDAC1/histone on chromatin contribute to the dynamic regulation of histone acetylation by balancing HDAC or KAT activity present at histones to reorganize chromatin structure and regulate transcription.

Indexed as

Gene Expression RegulationAcetylationAmino Acid SequenceBinding, CompetitiveBinding SitesCell Line, TumorChromatinEpithelial CellsHistone Deacetylase 1HistonesHumansMolecular Sequence Datap300-CBP-Associated Factorp300-CBP Transcription FactorsProtein BindingProtein Interaction Domains and MotifsChromatinHDAC1 protein, humanHistone Deacetylase 1Histonesp300-CBP-Associated Factorp300-CBP Transcription Factors

Identifiers

PMID24722339
PMCPMC3983199
OpenAlexW1976575536

What OpenQuestion 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 OpenQuestion graph.