NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.
Journal:
Nat. Struct. Mol. Biol. 2008 AugAuthors:
Zhou Z, Feng H, Hansen DF, Kato H, Luk E, Freedberg DI, Kay LE, Wu C, Bai Y
Abstract
The NMR structure of budding yeast chaperone Chz1 complexed with histones H2A.Z-H2B has been determined. Chz1 forms a long irregular chain capped by two short alpha-helices, and uses both positively and negatively charged residues to stabilize the histone dimer. A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions.
Mesh Headings:
Arginine, Carbon, Dimerization, Histone Chaperones, Histones, Lysine, Magnetic Resonance Spectroscopy, Molecular Chaperones, Molecular Conformation, Nitrogen, Nucleosomes, Protein Conformation, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Static Electricity