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- W2897943860 abstract "Abstract: Epigenetic regulation of the chromatin landscape is often orchestrated through modulation of nucleosomes. Nucleosomes are composed of two copies each of the four core histones, H2A, H2B, H3, and H4, wrapped in ~150 bp of DNA. We focus this review on recent structural studies that further elucidate the mechanisms used by macromolecular complexes to mediate histone modification and nucleosome assembly. Nucleosome assembly, spacing, and variant histone incorporation are coordinated by chromatin remodeler and histone chaperone complexes. Several recent structural studies highlight how disparate families of histone chaperones and chromatin remodelers share similar features that underlie how they interact with their respective histone or nucleosome substrates. Post‐translational modification of histone residues is mediated by enzymatic subunits within large complexes. Until recently, relatively little was known about how association with auxiliary subunits serves to modulate the activity and specificity of the enzymatic subunit. Analysis of several recent structures highlights the different modes that auxiliary subunits use to influence enzymatic activity or direct specificity toward individual histone residues." @default.
- W2897943860 created "2018-10-26" @default.
- W2897943860 creator A5022672117 @default.
- W2897943860 creator A5026532925 @default.
- W2897943860 creator A5049745445 @default.
- W2897943860 creator A5061620397 @default.
- W2897943860 date "2018-12-13" @default.
- W2897943860 modified "2023-10-11" @default.
- W2897943860 title "Molecular basis for chromatin assembly and modification by multiprotein complexes" @default.
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