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Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID
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SYSNO ASEP 0482733 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID Author(s) Gupta, K. (GB)
Wastson, A.A. (GB)
Baptista, T. (FR)
Scheer, E. (FR)
Chambers, A. (GB)
Koehler, CH. (DE)
Zou, J. (GB)
Obong-Ebong, I. (GB)
Kandiah, E. (FR)
Temblador, A. (FR)
Round, A. (FR)
Forest, E. (FR)
Man, Petr (MBU-M) RID, ORCID
Bienisssek, Ch. (FR)
Laue, E.D. (GB)
Lemke, E.A. (DE)
Rappsilber, J. (GB)
Robinson, C.V. (GB)
Devys, D. (FR)
Tora, L. (FR)
Berger, I. (US)Source Title eLife. - : eLife - ISSN 2050-084X
Roč. 6, e30395 (2017), s. 1-31Number of pages 31 s. Language eng - English Country GB - United Kingdom Keywords TATA-BINDING PROTEIN ; RNA-POLYMERASE-II ; CRYSTAL-STRUCTURE Subject RIV CE - Biochemistry OECD category Biochemistry and molecular biology Institutional support MBU-M - RVO:61388971 UT WOS 000415304700001 DOI 10.7554/eLife.30395 Annotation General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2018
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