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dc.contributor.authorWoodruff, Rachel V.
dc.contributor.authorBomar, Martha G.
dc.contributor.authorZhou, Pei
dc.contributor.authorWalker, Graham C.
dc.contributor.authorD'Souza, Sanjay Victor
dc.date.accessioned2015-10-07T15:18:04Z
dc.date.available2015-10-07T15:18:04Z
dc.date.issued2010-09
dc.date.submitted2010-07
dc.identifier.issn15687864
dc.identifier.urihttp://hdl.handle.net/1721.1/99180
dc.description.abstractRecent research has revealed the presence of ubiquitin-binding domains in the Y family polymerases. The ubiquitin-binding zinc finger (UBZ) domain of human polymerase η is vital for its regulation, localization, and function. Here, we elucidate structural and functional features of the non-canonical UBZ motif of Saccharomyces cerevisiae pol η. Characterization of pol η mutants confirms the importance of the UBZ motif and implies that its function is independent of zinc binding. Intriguingly, we demonstrate that zinc does bind to and affect the structure of the purified UBZ domain, but is not required for its ubiquitin-binding activity. Our finding that this unusual zinc finger is able to interact with ubiquitin even in its apo form adds support to the model that ubiquitin binding is the primary and functionally important activity of the UBZ domain in S. cerevisiae polymerase η. Putative ubiquitin-binding domains, primarily UBZs, are identified in the majority of known pol η homologs. We discuss the implications of our observations for zinc finger structure and pol η regulation.en_US
dc.description.sponsorshipNational Institute of Environmental Health Sciences (Grant ES-015818)en_US
dc.description.sponsorshipNational Institute of Environmental Health Sciences (Grant P30 ES-002109)en_US
dc.description.sponsorshipAmerican Cancer Society (Research Professorship)en_US
dc.language.isoen_US
dc.publisherElsevieren_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/j.dnarep.2010.08.001en_US
dc.rightsCreative Commons Attribution-Noncommercial-NoDerivativesen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.sourcePMCen_US
dc.titleThe unusual UBZ domain of Saccharomyces cerevisiae polymerase ηen_US
dc.typeArticleen_US
dc.identifier.citationWoodruff, Rachel V., Martha G. Bomar, Sanjay D’Souza, Pei Zhou, and Graham C. Walker. “The Unusual UBZ Domain of Saccharomyces Cerevisiae Polymerase η.” DNA Repair 9, no. 11 (November 2010): 1130–1141.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.mitauthorWoodruff, Rachel V.en_US
dc.contributor.mitauthorD'Souza, Sanjay Victoren_US
dc.contributor.mitauthorWalker, Graham C.en_US
dc.relation.journalDNA Repairen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsWoodruff, Rachel V.; Bomar, Martha G.; D'Souza, Sanjay; Zhou, Pei; Walker, Graham C.en_US
dc.identifier.orcidhttps://orcid.org/0000-0001-7243-8261
mit.licensePUBLISHER_CCen_US


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