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

Zheng Zhou; Hanqiao Feng; D. Flemming Hansen; Hidenori Kato; Ed Luk; Daron I. Freedberg; Lewis E. Kay; Carl Wu; Yawen Bai

doi:10.1038/nsmb.1465

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

Zheng Zhou
, Hanqiao Feng
, D. Flemming Hansen
, Hidenori Kato
, Ed Luk
, Daron I. Freedberg
, Lewis E. Kay
, Carl Wu
, Yawen Bai

Biochemistry and Cell Biology

National Institutes of Health
University of Toronto
United States Food and Drug Administration

Research output: Contribution to journal › Article › peer-review

89 Scopus citations

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 α-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.

Original language	English
Pages (from-to)	868-869
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	15
Issue number	8
DOIs	https://doi.org/10.1038/nsmb.1465
State	Published - Aug 2008

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10.1038/nsmb.1465

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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 α-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.",

author = "Zheng Zhou and Hanqiao Feng and Hansen, \{D. Flemming\} and Hidenori Kato and Ed Luk and Freedberg, \{Daron I.\} and Kay, \{Lewis E.\} and Carl Wu and Yawen Bai",

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AU - Zhou, Zheng

AU - Feng, Hanqiao

AU - Hansen, D. Flemming

AU - Kato, Hidenori

AU - Luk, Ed

AU - Freedberg, Daron I.

AU - Kay, Lewis E.

AU - Wu, Carl

AU - Bai, Yawen

PY - 2008/8

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N2 - 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 α-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.

AB - 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 α-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.

UR - https://www.scopus.com/pages/publications/49449114800

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DO - 10.1038/nsmb.1465

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AN - SCOPUS:49449114800

SN - 1545-9993

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EP - 869

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 8

ER -

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

Abstract

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