Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 25, Issue 13, Pages 5552-5566Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.25.13.5552-5566.2005
Keywords
-
Categories
Funding
- NCI NIH HHS [CA59936, R01 CA059936] Funding Source: Medline
- NIGMS NIH HHS [R37 GM062437, GM62437, R01 GM062437] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Ask authors/readers for more resources
Histone acetyltransferase (RAT) activities of proteins such as p300, CBP, and P/CAF play important roles in activation of gene expression. We now show that the HAT activity of p300 can also be required for down-regulation of transcription by a DNA binding repressor protein. Promyelocytic leukemia zinc finger (PLZF), originally identified as a fusion with retinoic acid receptor alpha in rare cases of all-trans-retinoic acid-resistant acute promyelocytic leukemia, is a transcriptional repressor that recruits histone deacetylase-containing corepressor complexes to specific DNA binding sites. PLZF associates with p300 in vivo, and its ability to repress transcription is specifically dependent on HAT activity of p300 and acetylation of lysines in its C-terminal C-2-H-2 zinc finger motif. An acetylation site mutant of PLZF does not repress transcription and is functionally deficient in a colony suppression assay despite retaining its abilities to interact with corepressor/histone deacetylase complexes. This is due to the fact that acetylation of PLZF activates its ability to bind specific DNA sequences both in vitro and in vivo. Taken together, our results indicate that a histone deacetylase-dependent transcriptional repressor can be positively regulated through acetylation and point to an unexpected role of a coactivator protein in transcriptional repression.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available