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dc.contributor.authorBrignole, Edward J.
dc.contributor.authorGibbons, Brian J.
dc.contributor.authorAzubel, Maia
dc.contributor.authorMurakami, Kenji
dc.contributor.authorVoss, Neil R.
dc.contributor.authorBushnell, David A.
dc.contributor.authorAsturias, Francisco J.
dc.contributor.authorKornberg, Roger D.
dc.date.accessioned2012-08-17T14:47:53Z
dc.date.available2012-08-17T14:47:53Z
dc.date.issued2012-01
dc.date.submitted2011-04
dc.identifier.issn0027-8424
dc.identifier.issn1091-6490
dc.identifier.urihttp://hdl.handle.net/1721.1/72183
dc.description.abstractStructures of complete 10-subunit yeast TFIIH and of a nested set of subcomplexes, containing 5, 6, and 7 subunits, have been determined by electron microscopy (EM) and 3D reconstruction. Consistency among all the structures establishes the location of the “minimal core” subunits (Ssl1, Tfb1, Tfb2, Tfb4, and Tfb5), and additional densities can be specifically attributed to Rad3, Ssl2, and the TFIIK trimer. These results can be further interpreted by placement of previous X-ray structures into the additional densities to give a preliminary picture of the RNA polymerase II preinitiation complex. In this picture, the key catalytic components of TFIIH, the Ssl2 ATPase/helicase and the Kin28 protein kinase are in proximity to their targets, downstream promoter DNA and the RNA polymerase C-terminal domain.en_US
dc.description.sponsorshipNational Cancer Institute (U.S.) (Grant number F32DK080622)en_US
dc.language.isoen_US
dc.publisherNational Academy of Sciencesen_US
dc.relation.isversionofhttp://dx.doi.org/10.1073/pnas.1105266109en_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.sourcePNASen_US
dc.titleSubunit architecture of general transcription factor TFIIHen_US
dc.typeArticleen_US
dc.identifier.citationGibbons, B. J. et al. “Subunit Architecture of General Transcription Factor TFIIH.” Proceedings of the National Academy of Sciences 109.6 (2012): 1949–1954. Copyright ©2012 by the National Academy of Sciencesen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.approverBrignole, Edward J.
dc.contributor.mitauthorBrignole, Edward J.
dc.relation.journalProceedings of the National Academy of Sciencesen_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.orderedauthorsGibbons, B. J.; Brignole, E. J.; Azubel, M.; Murakami, K.; Voss, N. R.; Bushnell, D. A.; Asturias, F. J.; Kornberg, R. D.en
mit.licensePUBLISHER_POLICYen_US
mit.metadata.statusComplete


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