Molecular basis for chromatin assembly and modification by multi-protein complexes.

Epigenetic regulation of the chromatin landscape is often orchestrated through modulation of nucleosomes. Nucleosomes are composed of 2 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 employed 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 employ to influence enzymatic activity or direct specificity towards individual histone residues. This article is protected by copyright. All rights reserved.