Recombinant PRC2 complex

Bromodomain-containing protein 7 (BRD7) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. Bromodomains function as 'readers' of these epigenetic histone marks and regulate chromatin structure and gene expression by linking associated proteins to the acetylated nucleosomal targets. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. The BET family consists of at least four members in mouse and human, BRD2 (also referred to as FSRG1, RING3), BRD3 (FSRG2, ORFX), BRD4 (FSRG4, MCAP/HUNK1), and BRDT (FSRG3, BRD6). BRD7 interacts with several proteins, including DVL1, PTPN13, IRF2 and HNRPUL1 and functions in the regulation of transcriptional activation and chromatin remodeling. Specifically, BRD7 has been shown to bind dishevelled-1 (DVL1) and enhance Wnt signaling via inhibition of GSK3b. BRD7 also associates with histones and E1B-AP5. In particular, it binds acetylated histone peptides, most notably H3 peptide acetylated at Lys14. BRD7 also inhibits G1-S progression by transcriptional regulation of molecules in the Ras and Rb pathways. BRD7 also suppresses tumorigenicity through binding and acetylation of p53 that results in efficient recruitment of p53 to target promoters and subsequent oncogene-induced senescence.