Acetylation of p65 at lysine 314 is important for late NF-kappaB-dependent gene expression.

ABSTRACT:

Background

NF-kappaB regulates the expression of a large number of target genes involved in the immune and inflammatory response, apoptosis, cell proliferation, differentiation and survival. We have earlier reported that p65, a subunit of NF-kappaB, is acetylated in vitro and in vivo at three different lysines (K310, K314 and K315) by the histone acetyltransferase p300.

Results

In this study, we describe that site-specific mutation of p65 at lysines 314 and 315 enhances gene expression of a subset of NF-kappaB target genes including Mmp10 and Mmp13. Increased gene expression was mainly observed three hours after TNFalpha stimulation. Chromatin immunoprecipitation (ChIP) experiments with an antibody raised against acetylated lysine 314 revealed that chromatin-bound p65 is ind

SUBMITTER: Rothgiesser KM 

PROVIDER: S-EPMC2823688 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature