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The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling.

Abstract : Histone variants within the H2A family show high divergences in their C-terminal regions. In this work, we have studied how these divergences and in particular, how a part of the H2A COOH-terminus, the docking domain, is implicated in both structural and functional properties of the nucleosome. Using biochemical methods in combination with Atomic Force Microscopy and Electron Cryo-Microscopy, we show that the H2A-docking domain is a key structural feature within the nucleosome. Deletion of this domain or replacement with the incomplete docking domain from the variant H2A.Bbd results in significant structural alterations in the nucleosome, including an increase in overall accessibility to nucleases, un-wrapping of ∼10 bp of DNA from each end of the nucleosome and associated changes in the entry/exit angle of DNA ends. These structural alterations are associated with a reduced ability of the chromatin remodeler RSC to both remodel and mobilize the nucleosomes. Linker histone H1 binding is also abrogated in nucleosomes containing the incomplete docking domain of H2A.Bbd. Our data illustrate the unique role of the H2A-docking domain in coordinating the structural-functional aspects of the nucleosome properties. Moreover, our data suggest that incorporation of a 'defective' docking domain may be a primary structural role of H2A.Bbd in chromatin.
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Manu Shubhdarshan Shukla, Sajad Hussain Syed, Damien Goutte-Gattat, John Lalith Charles Richard, Fabien Montel, et al.. The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling.. Nucleic Acids Research, Oxford University Press, 2011, 39 (7), pp.2559-70. ⟨10.1093/nar/gkq1174⟩. ⟨hal-00726345⟩



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