[NMR paper] NMR Analyses of Acetylated H2A.Z Isoforms Identify Differential Binding Interactions with the Bromodomain of the NURF Nucleosome Remodeling Complex.

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NMR Analyses of Acetylated H2A.Z Isoforms Identify Differential Binding Interactions with the Bromodomain of the NURF Nucleosome Remodeling Complex.

Related Articles NMR Analyses of Acetylated H2A.Z Isoforms Identify Differential Binding Interactions with the Bromodomain of the NURF Nucleosome Remodeling Complex.

Biochemistry. 2020 May 01;:

Authors: Olson N, Kroc S, Johnson J, Zahid H, Ycas PD, Chan A, Kimbrough J, Kalra P, Schönbrunn E, Pomerantz WCK

Abstract
Gene specific recruitment of bromodomain-containing proteins to chromatin is affected by post-translational acetylation of lysine on histones. Whereas bromodomain interactions with acetylation patterns of native histones (H2A, H2B, H3, and H4) have been well characterized, the recognition motif for histone variants H2A.Z I and H2A.Z II by bromodomains has yet to be fully investigated. Elucidating these molecular mechanisms is crucial for understanding transcriptional regulation in cellular processes involved in both development and disease. Here, we have used protein-observed fluorine NMR (PrOF NMR) to fully characterize the affinities of H2A.Z I and II acetylation patterns for BPTF's bromodomain, and found the diacetylated mark of lysine 7 and 13 on H2A.Z II to have the strongest interaction with K7ac preferentially engaging the binding site. We further paneled the selectivity of H2A.Z histones against a variety of bromodomains, revealing that the bromodomain of CECR2 binds with the highest affinity and specificity for acetylated H2A.Z I over isoform II. These results support a possible role for different H2A.Z transcriptional activation mechanisms through recruitment of chromatin remodeling complexes.


PMID: 32356653 [PubMed - as supplied by publisher]



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