期刊
MOLECULAR CELL
卷 27, 期 4, 页码 609-621出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.07.024
关键词
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资金
- NHLBI NIH HHS [R01 HL065445, R01 HL065445-09] Funding Source: Medline
- NIDDK NIH HHS [R37 DK039949, R37 DK039949-27] Funding Source: Medline
- NINDS NIH HHS [R01 NS048243, R01 NS048243-03] Funding Source: Medline
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.
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