Počet záznamů: 1
Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID
- 1.0482733 - MBU-M 2018 RIV GB eng J - Článek v odborném periodiku
Gupta, K. - Wastson, A.A. - Baptista, T. - Scheer, E. - Chambers, A. - Koehler, CH. - Zou, J. - Obong-Ebong, I. - Kandiah, E. - Temblador, A. - Round, A. - Forest, E. - Man, Petr - Bienisssek, Ch. - Laue, E.D. - Lemke, E.A. - Rappsilber, J. - Robinson, C.V. - Devys, D. - Tora, L. - Berger, I.
Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.
eLife. Roč. 6, e30395 (2017), s. 1-31. ISSN 2050-084X
Institucionální podpora: RVO:61388971
Klíčová slova: TATA-BINDING PROTEIN * RNA-POLYMERASE-II * CRYSTAL-STRUCTURE
Kód oboru RIV: CE - Biochemie
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 7.616, rok: 2017
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.
Trvalý link: http://hdl.handle.net/11104/0278200