期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 26, 页码 23388-23396出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.207407
关键词
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资金
- Marie Curie Framework Program
- European Molecular Biology Organization
- European Molecular Biology Laboratory/European Synchrotron Radiation Facility Joint Structural Biology Group
Drosophila Nurf55 is a component of different chromatin-modifying complexes, including the PRC2(Polycomb repressive complex 2). Based on the 1.75-angstrom crystal structure of Nurf55 bound to histone H4 helix 1, we analyzed interactions of Nurf55 (Nurf55 or p55 in fly and 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 pulldown experiments. Site-directed mutagenesis identified the binding site of histone H3 at the top of the Nurf55 WD40 propeller. Unmodified or K9me3- or K27me3-containing H3 peptides were bound with similar affinities, whereas the affinity for K4me3-containing H3 peptides was reduced. Helix 1 of histone H4 and Su(z) 12 bound 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.
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