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Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID

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...

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Detalles Bibliográficos
Autores principales: Gupta, Kapil, Watson, Aleksandra A, Baptista, Tiago, Scheer, Elisabeth, Chambers, Anna L, Koehler, Christine, Zou, Juan, Obong-Ebong, Ima, Kandiah, Eaazhisai, Temblador, Arturo, Round, Adam, Forest, Eric, Man, Petr, Bieniossek, Christoph, Laue, Ernest D, Lemke, Edward A, Rappsilber, Juri, Robinson, Carol V, Devys, Didier, Tora, Làszlò, Berger, Imre
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5690282/
https://www.ncbi.nlm.nih.gov/pubmed/29111974
http://dx.doi.org/10.7554/eLife.30395
Descripción
Sumario: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.