Architecture of TAF11/TAF13/TBP complex suggests novel regulatory state of human general transcription factor TFIID

ABSTRACT: General transcription factor TFIID is a key component of RNA polymerase II transcription initiation in eukaryotic nuclei. Human TFIID is a megadalton-sized multiprotein complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. A number of transcription regulatory factors were found to compete with DNA for TBP binding. 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. In an integrative approach combing 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. Our results thus suggest a novel regulatory state for TFIID function.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture, Permanent Cell Line Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Luc Negroni  

LAB HEAD: Tora Laszlo

PROVIDER: PXD005676 | Pride | 2017-11-15

REPOSITORIES: Pride