Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange

Wei Hua Wu, Samar Alami, Edward Luk, Chwen Huey Wu, Subhojit Sen, Gaku Mizuguchi, Debbie Wei, Carl Wu

    Research output: Contribution to journalArticle

    166 Scopus citations

    Abstract

    The histone variant H2AZ is incorporated preferentially at specific locations in chromatin to modulate chromosome functions. In Saccharomyces cerevisiae, deposition of histone H2AZ is mediated by the multiprotein SWR1 complex, which catalyzes ATP-dependent exchange of nucleosomal histone H2A for H2AZ. Here, we define interactions between SWR1 components and H2AZ, revealing a link between the ATPase domain of Swr1 and three subunits required for the binding of H2AZ. We discovered that Swc2 binds directly to and is essential for transfer of H2AZ. Swc6 and Arp6 are necessary for the association of Swc2 and for nucleosome binding, whereas other subunits, Swc5 and Yaf9, are required for H2AZ transfer but neither H2AZ nor nucleosome binding. Finally, the C-terminal α-helix of H2AZ is crucial for its recognition by SWR1. These findings provide insight on the initial events of histone exchange.

    Original languageEnglish (US)
    Pages (from-to)1064-1071
    Number of pages8
    JournalNature Structural and Molecular Biology
    Volume12
    Issue number12
    DOIs
    Publication statusPublished - Dec 27 2005

      Fingerprint

    ASJC Scopus subject areas

    • Structural Biology
    • Molecular Biology

    Cite this

    Wu, W. H., Alami, S., Luk, E., Wu, C. H., Sen, S., Mizuguchi, G., ... Wu, C. (2005). Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nature Structural and Molecular Biology, 12(12), 1064-1071. https://doi.org/10.1038/nsmb1023