Bromodomain proteins are part of the transcriptional mediator family, with a role in recruiting RNA pol II (Gibbons, et al., 2019). This model demonstrates the structural interactions between the BD1 bromodomain of BRDT and the hyper-acetylated, H4K5acK8ac histone. The interaction between BD1 and the hyper-acetylated histone tails is focal in chromatin remodelling prior to the final stages of sperm differentiation in spermatogenesis, in which acetylated histones are in their active form (Moriniere etal., 2009). BRDT functions post-meiotic division of sperm, where it localizes to the nucleus and reorganizes histones, through this hyper-acetylation recognition pathway (Matzuk et al., 2012). This tour begins with a look at the binding pocket of BDRT, consisting of a short BC, and long ZA chain, as well as looking into what defines the pockets binding accommodation. This is followed by a look into specific binding of the K8ac chain, and finally a possible use of bromo domain inhibitors in male contraception.
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