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

Autor: 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
Přispěvatelé: European Molecular Biology Laboratory [Grenoble] (EMBL), Department of Biochemistry [Cambridge], University of Cambridge [UK] (CAM), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), BrisSynBio Centre, The School of Biochemistry, University of Bristol [Bristol], European Molecular Biology Laboratory [Heidelberg] (EMBL), Wellcome Trust Centre for Cell Biology, University of Edinburgh, Physical and Theoretical ChemistryLaboratory, University of Oxford [Oxford], Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institute of Microbiology of the Czech Academy of Sciences (MBU / CAS), Czech Academy of Sciences [Prague] (CAS), Department of Chemistry, University of Oxford, University of Oxford [Oxford]-Chemistry Research Laboratory, University of Oxford, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institute of Microbiology of the Czech Academy of Sciences [Prague, Czech Republic] (MBU / CAS), University of Oxford-Chemistry Research Laboratory, Chambers, Anna L [0000-0001-8133-6240], Temblador, Arturo [0000-0003-3076-6317], Laue, Ernest D [0000-0002-7476-4148], Devys, Didier [0000-0001-9655-3512], Tora, Làszlò [0000-0001-7398-2250], Berger, Imre [0000-0001-7518-9045], Apollo - University of Cambridge Repository
Rok vydání: 2017
Předmět:
MESH: TFIID
Protein Conformation
Structural Biology and Molecular Biophysics
genetic processes
MESH: biophysics
S. cerevisiae
MESH: biochemistry
MESH: transcription factors
Crystallography
X-Ray
TBP associated factors
Mass Spectrometry
MESH: histone fold domain
MESH: human
biophysics
Protein Interaction Mapping
structural biology
Biology (General)
Promoter Regions
Genetic
Histone Acetyltransferases
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
TFIID
MESH: TBP associated factors
Medicine
Protein Binding
Research Article
Human
QH301-705.5
MESH: structural biology
Science
information science
MESH: core promoter DNA
macromolecular substances
histone fold domain
Biochemistry and Chemical Biology
transcription factors
biochemistry
Humans
MESH: gene regulation
TATA-Binding Protein Associated Factors
Bristol BioDesign Institute
core promoter DNA
DNA
TATA-Box Binding Protein
SYNTHETIC BIOLOGY
enzymes and coenzymes (carbohydrates)
health occupations
MESH: S. cerevisiae
Transcription Factor TFIID
gene regulation
Zdroj: eLife
'eLife ', vol: 6, pages: e30395-1-e30395-31 (2017)
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, ' Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID ', eLife, vol. 6, e30395 . https://doi.org/10.7554/eLife.30395
eLife, eLife Sciences Publication, 2017, 6, ⟨10.7554/eLife.30395⟩
eLife, Vol 6 (2017)
eLife, 2017, 6, ⟨10.7554/eLife.30395⟩
ISSN: 2050-084X
DOI: 10.7554/eLife.30395
Popis: International audience; 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.
Databáze: OpenAIRE
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