RT Journal Article
SR Electronic
T1 Architecture of TAF11/TAF13/TBP complex suggests novel regulatory state in General Transcription Factor TFIID function
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 168716
DO 10.1101/168716
A1 Kapil Gupta
A1 Aleksandra A. Watson
A1 Tiago Baptista
A1 Elisabeth Scheer
A1 Anna L. Chambers
A1 Christine Koehler
A1 Juan Zou
A1 Ima Obong-Ebong
A1 Eaazhisai Kandiah
A1 Arturo Temblador
A1 Adam Round
A1 Eric Forest
A1 Petr Man
A1 Christoph Bieniossek
A1 Ernest D. Laue
A1 Edward A. Lemke
A1 Juri Rappsilber
A1 Carol V. Robinson
A1 Didier Devys
A1 Laszlo Tora
A1 Imre Berger
YR 2017
UL http://biorxiv.org/content/early/2017/07/26/168716.abstract
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.