2xyi
Crystal Structure of Nurf55 in complex with a H4 peptide
Structural highlights
FunctionCAF1_DROME Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.[1] [2] [3] [4] [5] Publication Abstract from PubMedDrosophila Nurf55 is a component of different chromatin-modifying complexes including the Polycomb Repressive Complex 2 (PRC2). Based on the 1.75 A crystal structure of Nurf55 bound to histone H4 helix 1, we analyzed interactions of Nurf55 (Nurf55 or p55 in fly, RbAp48/46 in human) with the N-terminal tail of histone H3, the first helix of histone H4 and an N-terminal fragment of the PRC2 subunit Su(z)12 using isothermal calorimetry and pull-down experiments. Site-directed mutagenesis identified the binding site of histone H3 at the top of the Nurf55 WD40 propeller. Unmodified, K9me3 or K27me3 containing H3 peptides are bound with similar affinities, while the affinity for K4me3 containing H3 peptides is reduced. Helix 1 of histone H4 and Su(z)12 bind to the edge of the beta-propeller using overlapping binding sites. Our results show similarities in the recognition of histone H4 and Su(z)12 and identify Nurf55 as a versatile interactor that simultaneously contacts multiple partners. Chromatin-modifying complex component Nurf55/p55 associates with histones H3, H4 and Polycomb Repressive Complex 2 subunit Su(z)12 through partially overlapping binding sites.,Nowak AJ, Alfieri C, Stirnimann CU, Rybin V, Baudin F, Ly-Hartig N, Lindner D, Muller CW J Biol Chem. 2011 May 5. PMID:21550984[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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