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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z

Nature Structural Biology volume 7, pages 1121–1124 (2000)Cite this article

Abstract

Activation of transcription within chromatin has been correlated with the incorporation of the essential histone variant H2A.Z into nucleosomes. H2A.Z and other histone variants may establish structurally distinct chromosomal domains; however, the molecular mechanism by which they function is largely unknown. Here we report the 2.6 Å crystal structure of a nucleosome core particle containing the histone variant H2A.Z. The overall structure is similar to that of the previously reported 2.8 Å nucleosome structure containing major histone proteins. However, distinct localized changes result in the subtle destabilization of the interaction between the (H2A.Z–H2B) dimer and the (H3–H4)2 tetramer. Moreover, H2A.Z nucleosomes have an altered surface that includes a metal ion. This altered surface may lead to changes in higher order structure, and/or could result in the association of specific nuclear proteins with H2A.Z. Finally, incorporation of H2A.Z and H2A within the same nucleosome is unlikely, due to significant changes in the interface between the two H2A.Z–H2B dimers.

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Figure 1: Overall comparison of H2A.Z-NCP and major-NCP.
Figure 2: The docking domain.
Figure 3: The electrostatic potentials of nucleosomal surfaces.
Figure 4: The L1 loop.

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Acknowledgements

We thank T. Earnest at the Advanced Light Source in Berkeley for support and cooperation; W. Schreurs, M. Schnizer and E. Schonbrunn (Colorado State University) for technical support; and V. Roberts (the Scripps Research Institute) for help with Fig. 3. This work was supported in part by a Searle Scholar Award to K.L., by the Cancer League of Colorado, by the Graduate School of Colorado State University, and by the Basil O'Conner Starter Scholar Award from the March of Dimes to K.L.

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Authors and Affiliations

  1. Department of Biochemistry Molecular Biology, Colorado State University, Fort Collins, 80523-1870 , Colorado, USA

    Robert K. Suto & Karolin Luger

  2. The John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra Australian Capital Territory, 2601, Australia

    Michael J. Clarkson & David J. Tremethick

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  1. Robert K. Suto
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Correspondence to Karolin Luger.

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Suto, R., Clarkson, M., Tremethick, D. et al. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat Struct Mol Biol 7, 1121–1124 (2000). https://doi.org/10.1038/81971

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