Download MendeleyArchitecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.
Gupta, K., Watson, A.A., Baptista, T., Scheer, E., Chambers, A.L., Koehler, C., Zou, J., Obong-Ebong, I., Kandiah, E., Temblador, A., Round, A., Forest, E., Man, P., Bieniossek, C., Laue, E.D., Lemke, E.A., Rappsilber, J., Robinson, C.V., Devys, D., Tora, L., Berger, I.(2017) Elife 6
- PubMed: 29111974
- DOI: https://doi.org/10.7554/eLife.30395
- Primary Citation of Related Structures:
5M4S - PubMed Abstract:
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.
Organizational Affiliation:
BrisSynBio Centre, The School of Biochemistry, Faculty of Biomedical Sciences, University of Bristol, Bristol, United Kingdom.
