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

被引：85

作者：

Zhou, Zheng ^{[1
]}

Feng, Hanqiao ^{[1
]}

Hansen, D. Flemming ^{[2
]}

Kato, Hidenori ^{[1
]}

Luk, Ed ^{[1
]}

Freedberg, Daron I. ^{[3
]}

Kay, Lewis E. ^{[2
]}

Wu, Carl ^{[1
]}

Bai, Yawen ^{[1
]}

机构：

[1] NCI, Biochem & Mol Biol Lab, Ctr Canc Res, NIH, Bethesda, MD 20892 USA

[2] Univ Toronto, Dept Med Genet Biochem & Chem, Toronto, ON M5S 1A8, Canada

[3] US FDA, NMR Spect Lab Bacterial Polysaccharides, Ctr Biol Evaluat & Res, Bethesda, MD 20892 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 08期

关键词：

D O I：

10.1038/nsmb.1465

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：868 / 869

页数：2

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