PT  - JOURNAL ARTICLE
AU  - Kapil Gupta
AU  - Aleksandra A. Watson
AU  - Tiago Baptista
AU  - Elisabeth Scheer
AU  - Anna L. Chambers
AU  - Christine Koehler
AU  - Juan Zou
AU  - Ima Obong-Ebong
AU  - Eaazhisai Kandiah
AU  - Arturo Temblador
AU  - Adam Round
AU  - Eric Forest
AU  - Petr Man
AU  - Christoph Bieniossek
AU  - Ernest D. Laue
AU  - Edward A. Lemke
AU  - Juri Rappsilber
AU  - Carol V. Robinson
AU  - Didier Devys
AU  - Laszlo Tora
AU  - Imre Berger
TI  - Architecture of TAF11/TAF13/TBP complex suggests novel regulatory state in General Transcription Factor TFIID function
AID  - 10.1101/168716
DP  - 2017 Jan 01
TA  - bioRxiv
PG  - 168716
4099  - http://biorxiv.org/content/early/2017/07/26/168716.short
4100  - http://biorxiv.org/content/early/2017/07/26/168716.full
AB  - 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-binding 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.