Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation.

ABSTRACT: p300/cyclic AMP-responsive element binding protein-binding protein (CBP) are general coactivators for multiple transcription factors involved in various cellular processes. Several highly conserved domains of p300/CBP serve as interacting sites for transcription factors and regulatory proteins. Particularly, the intrinsic histone acetyltransferase (HAT) activity and transactivation domains (TAD) play essential roles for their coactivating function. Autoacetylation of p300/CBP is commonly observed in cell-free HAT assays and has been implicated in the regulation of their HAT activity. Here, we show that six lysine-rich regions in several highly conserved functional domains of p300 are targeted by p300HAT for acetylation in cell-free systems. We show that p300 is susceptible to acetylation i

SUBMITTER: Stiehl DP 

PROVIDER: S-EPMC4526273 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature