期刊
GENES & DEVELOPMENT
卷 16, 期 24, 页码 3130-3135出版社
COLD SPRING HARBOR LAB PRESS
DOI: 10.1101/gad.1037502
关键词
histone deacetylase; TRiC; SMRT; N-CoR; corepressor; HDAC3
资金
- NCI NIH HHS [P30 CA006927, CA06927] Funding Source: Medline
- NIDDK NIH HHS [R37 DK043806, DK43806, R01 DK045586, DK45586] Funding Source: Medline
The acetylation of historic tails is a primary determinant of gene activity. Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity. Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process. SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme. The SMRT-HDAC3 repression complex thus joins the VHL-elongin BC tumor suppression complex and the cyclin E-Cdk2 cell cycle regulation complex as critical cellular machines requiring TRiC for proper assembly and function. The strict control of HDAC3 activity underscores the cellular imperative that histone deacetylation occur only in targeted regions of the genome.
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