作 者：Su Qin, Lei Jin, Jiahai Zhang, Lei Liu, Peng Ji, Mian Wu, Jihui Wu and Yunyu Shi,
Abstract：MOZ (monocytic leukemic zinc-finger protein) and MORF (MOZ-related factor) are histone acetyltransferases important for HOX gene expression as well as embryo and postnatal development. They form complexes with other regulatory subunits through the scaffold proteins BRPF1/2/3 (Bromodomain-PHD finger proteins 1, 2 or 3). BRPF proteins have multiple domains,
including two PHD fingers, for potential interactions with histones. Here, we show that the first PHD finger of BRPF2 specifically recognizes the N-terminal tail of unmodified histone H3 (unH3) and reportthe solution structures of this PHD finger, both free and in complex with the unH3 peptide. Structural analysis revealed that the unH3 peptide forms a third antiparallel β-strand that pairs with the PHD1’s two-stranded antiparallel?β-sheet. The binding specificity was determined primarily through the recognition of arginine 2 and lysine 4 of the unH3 by conserved aspartic acids of PHD1 and of threonine 6 of the unH3 by a conserved asparagine. ITC and NMR assays showed that post-translational modifications, such as H3R2me2as, H3T3ph, H3K4me, H3K4ac and H3T6ph, antagonized the interactionbetween histone H3 and PHD1. Furthermore, histone binding by PHD1 was important for BRPF2 to localize to the HOXA9?locus?in vivo. PHD1 is highly conserved in yeast NuA3 and other histone acetyltransferase complexes, so the results reported here also shed light on the function and regulation of these complexes.
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