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

Nature Structural & Molecular Biology volume 15, pages 868–869 (2008)Cite this article

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.

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Figure 1: Structure and dynamics of the CZB complex.
Figure 2: Electrostatic interactions between the Chz core and sH2B_H2A.Z. lysine and arginine are shown with blue dotted surfaces for the nitrogen and carbon atoms.

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Acknowledgements

We thank A. Bax, C. Klee and M. Lichten for comments. This work was supported by the intramural program of the US National Cancer Institute (C.W. and Y.B.) and a grant from the Canadian Institutes of Health Research (L.E.K.). D.F.H. is the recipient of a postdoctoral fellowship from the Danish Agency for Science, Technology and Innovation.

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Author notes

  1. Zheng Zhou and Hanqiao Feng: These authors contributed equally to this work.

Authors and Affiliations

  1. Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, 20892, Maryland, USA

    Zheng Zhou, Hanqiao Feng, Hidenori Kato, Ed Luk, Carl Wu & Yawen Bai

  2. Department of Medical Genetics, Biochemistry and Chemistry, University of Toronto, 1 King's College Circle, Toronto, M5S 1A8, Ontario, Canada

    D Flemming Hansen & Lewis E Kay

  3. NMR Spectroscopy Laboratory of Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, 20892, Maryland, USA

    Daron I Freedberg

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  1. Zheng Zhou
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Correspondence to Yawen Bai.

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Supplementary Figures 1–6, Supplementary Table 1 and Supplementary Methods (PDF 2979 kb)

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Zhou, Z., Feng, H., Hansen, D. et al. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B. Nat Struct Mol Biol 15, 868–869 (2008). https://doi.org/10.1038/nsmb.1465

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