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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

Authors

  • Zhou Z
  • Feng H
  • Hansen DF
  • Kato H
  • Luk E
  • Freedberg DI
  • Kay LE
  • Wu C
  • Bai Y

Journal

Nature structural & molecular biology

Publication Data

August 5, 2008

Associated Grants

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

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