| Summary: | <p>Abstract</p> <p>Background</p> <p>NF-κB 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-κB, is acetylated <it>in vitro </it>and <it>in vivo </it>at three different lysines (K310, K314 and K315) by the histone acetyltransferase p300.</p> <p>Results</p> <p>In this study, we describe that site-specific mutation of p65 at lysines 314 and 315 enhances gene expression of a subset of NF-κB target genes including <it>Mmp10 </it>and <it>Mmp13</it>. Increased gene expression was mainly observed three hours after TNFα stimulation. Chromatin immunoprecipitation (ChIP) experiments with an antibody raised against acetylated lysine 314 revealed that chromatin-bound p65 is indeed acetylated at lysine 314.</p> <p>Conclusions</p> <p>Together, our results establish acetylation of K314 as an important regulatory modification of p65 and subsequently of NF-κB-dependent gene expression.</p>
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