Biological function and histone recognition of family IV bromodomain-containing proteins

Journal of Cellular Physiology
Jonathan T Lloyd, Karen C Glass

Abstract

Bromodomain proteins function as epigenetic readers that recognize acetylated histone tails to facilitate the transcription of target genes. There are approximately 60 known human bromodomains, which are divided into eight sub-families based on structural conservation. The bromodomain-containing proteins in family IV include seven members (BRPF1, BRPF2, BRPF3, BRD7, BRD9, ATAD2, and ATAD2b). The bromodomains of each of these proteins recognize and bind acetyllysine residues on histone tails protruding from the nucleosome. However, the histone marks recognized by each bromodomain protein can be very different. The BRPF1 subunit of the MOZ histone acetyltransferase (HAT) recognizes acetylated histones H2AK5ac, H4K12ac, H3K14ac, H4K8ac, and H4K5ac. While the bromodomain of BRD7, a member of the SWI/SNF complex, was shown to preferentially recognize acetylated histones H3K9ac, H3K14ac, H4K8ac, H4K12ac, and H4K16ac. The bromodomains of BRPF2 and BRPF3 have similar sequences, and function as part of the HBO1 HAT complex, but there is limited data on which histone ligands they bind. Similarly, there is little known about the histone targets of the BRD9 and ATAD2b bromodomain proteins. Interestingly, the ATAD2 bromodomain was recently ...Continue Reading

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Jun 13, 2018·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·Yukihiro Itoh
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Oct 19, 2017·ACS Chemical Biology·Amaury E Fernández-MontalvánMátyás Gorjánácz
Oct 22, 2020·Journal of Medicinal Chemistry·Jonathan T LloydKaren C Glass

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