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Significance The Polycomb protein (PC) is well known for its role in transcriptional silencing and binding to trimethylated histone H3 Lys27 (H3K27me3). We report here that PC inhibits the histone acetyltransferase (HAT) activity of CREB-binding protein (CBP). PC interacts directly with the CBP HAT domain, binding to its autoregulatory loop, whose autoacetylation greatly enhances enzyme activity. PC binding inhibits histone H3 acetylation. Interestingly, CBP autoacetylation impairs PC binding in vitro, and PC is preferentially associated with unacetylated CBP in vivo. Altering PC levels in vivo alters the acetylated H3K27 (H3K27ac) level in a predictable manner. PC inhibition of CBP HAT activity at enhancers and promoters with paused RNA polymerase II may affect regulation of both repressed and active genes.

Polycomb inhibits histone acetylation by CBP by binding directly to its catalytic domain