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Cryo-EM Reveals Promoter DNA Binding and Conformational Flexibility of the General Transcription Factor TFIID
Vise andre og tillknytning
2009 (engelsk)Inngår i: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 17, nr 11, s. 1442-1452Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the THID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions.

sted, utgiver, år, opplag, sider
2009. Vol. 17, nr 11, s. 1442-1452
Emneord [en]
rna-polymerase-ii, tata box, crystal-structure, preinitiation complex, minor-groove, yeast, protein, tbp, tafs, subunit
Identifikatorer
URN: urn:nbn:se:kth:diva-18975DOI: 10.1016/j.str.2009.09.007ISI: 000272011500006OAI: oai:DiVA.org:kth-18975DiVA, id: diva2:337022
Merknad
QC 20100525Tilgjengelig fra: 2010-08-05 Laget: 2010-08-05 Sist oppdatert: 2017-12-12bibliografisk kontrollert

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