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dc.contributor.authorNishino, Tatsuya
dc.contributor.authorTakeuchi, Kozo
dc.contributor.authorGascoigne, Karen E.
dc.contributor.authorSuzuki, Aussie
dc.contributor.authorHori, Tetsuya
dc.contributor.authorOyama, Takuji
dc.contributor.authorMorikawa, Kosuke
dc.contributor.authorFukagawa, Tatsuo
dc.contributor.authorCheeseman, Iain McPherson
dc.date.accessioned2014-01-27T17:22:03Z
dc.date.available2014-01-27T17:22:03Z
dc.date.issued2012-02
dc.date.submitted2011-08
dc.identifier.issn00928674
dc.identifier.issn1097-4172
dc.identifier.urihttp://hdl.handle.net/1721.1/84581
dc.description.abstractThe multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the “histone code” beyond canonical nucleosome proteins.en_US
dc.description.sponsorshipKinship Foundation. Searle Scholars Programen_US
dc.description.sponsorshipNational Institute of General Medical Sciences (U.S.) (Grant GM088313)en_US
dc.language.isoen_US
dc.publisherElsevieren_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/j.cell.2011.11.061en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceElsevier Open Archiveen_US
dc.titleCENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Folden_US
dc.typeArticleen_US
dc.identifier.citationNishino, Tatsuya, Kozo Takeuchi, Karen E. Gascoigne, Aussie Suzuki, Tetsuya Hori, Takuji Oyama, Kosuke Morikawa, Iain M. Cheeseman, and Tatsuo Fukagawa. “CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold.” Cell 148, no. 3 (February 2012): 487-501. Copyright © 2012 Elsevier Inc.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentWhitehead Institute for Biomedical Researchen_US
dc.contributor.mitauthorGascoigne, Karen E.en_US
dc.contributor.mitauthorCheeseman, Iain McPhersonen_US
dc.relation.journalCellen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsNishino, Tatsuya; Takeuchi, Kozo; Gascoigne, Karen E.; Suzuki, Aussie; Hori, Tetsuya; Oyama, Takuji; Morikawa, Kosuke; Cheeseman, Iain M.; Fukagawa, Tatsuoen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-3829-5612
mit.licensePUBLISHER_POLICYen_US


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