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

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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.

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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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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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