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.
Zhou
Zheng
Z
Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Feng
Hanqiao
H
Hansen
D Flemming
DF
Kato
Hidenori
H
Luk
Ed
E
Freedberg
Daron I
DI
Kay
Lewis E
LE
Wu
Carl
C
Bai
Yawen
Y
D001120:Arginine / Q000737:chemistry; D002244:Carbon / Q000737:chemistry; D019281:Dimerization; D056488:Histone Chaperones; D006657:Histones / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D018832:Molecular Chaperones / Q000737:chemistry*; D008968:Molecular Conformation; D009584:Nitrogen / Q000737:chemistry; D009707:Nucleosomes / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D055672:Static Electricity
C518297:Chz1 protein, S cerevisiae; D056488:Histone Chaperones; D006657:Histones; C493530:Htz1 protein, S cerevisiae; D018832:Molecular Chaperones; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D002244:Carbon; D001120:Arginine; D008239:Lysine; D009584:Nitrogen