INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/ncomms15616.pdf
Reference74 articles.
1. Guillemette, B. & Gaudreau, L. Reuniting the contrasting functions of H2A.Z. Biochem. Cell Biol. 84, 528–535 (2006).
2. Mizuguchi, G. et al. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303, 343–348 (2004).
3. Suto, R. K., Clarkson, M. J., Tremethick, D. J. & Luger, K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 7, 1121–1124 (2000).
4. Park, Y. J., Dyer, P. N., Tremethick, D. J. & Luger, K. A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J. Biol. Chem. 279, 24274–24282 (2004).
5. Fan, J. Y., Rangasamy, D., Luger, K. & Tremethick, D. J. H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding. Mol. Cell 16, 655–661 (2004).
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