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A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation.

Deciphering the epigenetic "code" remains a central issue in transcriptional regulation. Here, we report the identification of a JAMM/MPN(+) domain-containing histone H2A deubiquitinase (2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A) that has permitted delineation of a strategy for specific regulatory pathways of gene activation. 2A-DUB regulates transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF in a coregulatory protein complex, with its deubiquitinase activity modulated by the status of acetylation of nucleosomal histones. Consistent with this mechanistic role, 2A-DUB participates in transcriptional regulation events in androgen receptor-dependent gene activation, and the levels of uH2A are dramatically decreased in prostate tumors, serving as a cancer-related mark. We suggest that H2A ubiquitination represents a widely used mechanism for many regulatory transcriptional programs and predict that various H2A ubiquitin ligases/deubiquitinases will be identified for specific cohorts of regulated transcription units.

Pubmed ID: 17707232


  • Zhu P
  • Zhou W
  • Wang J
  • Puc J
  • Ohgi KA
  • Erdjument-Bromage H
  • Tempst P
  • Glass CK
  • Rosenfeld MG


Molecular cell

Publication Data

August 17, 2007

Associated Grants

  • Agency: NHLBI NIH HHS, Id: R01 HL065445
  • Agency: NHLBI NIH HHS, Id: R01 HL065445-09
  • Agency: NINDS NIH HHS, Id: R01 NS048243
  • Agency: NINDS NIH HHS, Id: R01 NS048243-03
  • Agency: NIDDK NIH HHS, Id: R37 DK039949
  • Agency: NIDDK NIH HHS, Id: R37 DK039949-27

Mesh Terms

  • Acetylation
  • Androgens
  • Animals
  • Cell Line
  • Chromatography, Affinity
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • Histone Acetyltransferases
  • Histones
  • Humans
  • Mice
  • Models, Genetic
  • Nucleosomes
  • Phosphorylation
  • Receptors, Androgen
  • Signal Transduction
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation
  • Ubiquitins