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.
Publication types
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Arginine / chemistry
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Carbon / chemistry
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Dimerization
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Histone Chaperones
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Histones / chemistry*
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Lysine / chemistry
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Magnetic Resonance Spectroscopy / methods*
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Molecular Chaperones / chemistry*
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Molecular Conformation
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Nitrogen / chemistry
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Nucleosomes / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry*
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Static Electricity
Substances
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Chz1 protein, S cerevisiae
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Histone Chaperones
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Histones
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Htz1 protein, S cerevisiae
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Molecular Chaperones
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Nucleosomes
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Saccharomyces cerevisiae Proteins
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Carbon
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Arginine
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Lysine
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Nitrogen