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NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.

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.

Pubmed ID: 18641662 RIS Download

Mesh terms: 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

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Associated grants

  • Agency: Intramural NIH HHS, Id: Z01 BC010808-01

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