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dc.creatorChen, Lu
dc.creatorConaway, Ronald C.
dc.creatorConaway, Joan W.
dc.date.accessioned2023-10-27T20:14:06Z
dc.date.available2023-10-27T20:14:06Z
dc.date.issued2013-12-02
dc.identifier.citationChen L, Conaway RC, Conaway JW. Multiple modes of regulation of the human Ino80 SNF2 ATPase by subunits of the INO80 chromatin-remodeling complex. Proc. Natl. Acad. Sci. 2013 Dec 2;110(51):20497-20502. doi:10.1073/pnas.1317092110.
dc.identifier.issn1091-6490
dc.identifier.urihttp://hdl.handle.net/20.500.12613/9103
dc.description.abstractSNF2 family ATPases are ATP-dependent motors that often function in multisubunit complexes to regulate chromatin structure. Although the central role of SNF2 ATPases in chromatin biology is well established, mechanisms by which their catalytic activities are regulated by additional subunits of chromatin-remodeling complexes are less well understood. Here we present evidence that the human Inositol auxotrophy 80 (Ino80) SNF2 ATPase is subject to regulation at multiple levels in the INO80 chromatin-remodeling complex. The zinc finger histidine triad domain-containing protein Ies2 (Ino Eighty Subunit 2) functions as a potent activator of the intrinsic catalytic activity of the Ino80 ATPase, whereas the YL-1 family Ies6 (Ino Eighty Subunit 6) and actin-related Arp5 proteins function together to promote binding of the Ino80 ATPase to nucleosomes. These findings support the idea that both substrate recognition and the intrinsic catalytic activities of SNF2 ATPases have evolved as important sites for their regulation.
dc.format.extent8 pages
dc.languageEnglish
dc.language.isoeng
dc.relation.ispartofFaculty/ Researcher Works
dc.relation.haspartProceedings of the National Academy of Sciences (PNAS), Vol. 110, No. 51
dc.relation.isreferencedby© 2013 National Academy of Sciences.
dc.rightsAll Rights Reserved
dc.titleMultiple modes of regulation of the human Ino80 SNF2 ATPase by subunits of the INO80 chromatin-remodeling complex
dc.typeText
dc.type.genrePost-print
dc.contributor.groupLu Chen Lab (Temple University)
dc.contributor.groupFox Chase Cancer Center
dc.description.departmentCancer and Cellular Biology
dc.relation.doihttps://doi.org/10.1073/pnas.1317092110
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.description.schoolcollegeLewis Katz School of Medicine
dc.creator.orcidChen|0000-0002-4571-7975
dc.temple.creatorChen, Lu
refterms.dateFOA2023-10-27T20:14:06Z


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