Chaperonin CCT Checkpoint Function in Basal Transcription Factor TFIID Assembly

Autor: Antonova, Simona V, Haffke, Matthias, Corradini, Eleonora, Mikuciunas, Mykolas, Low, Teck Y, Signor, Luca, van Es, Robert M, Gupta, Kapil, Scheer, Elisabeth, Vos, Harmjan R, Tora, László, Heck, Albert J R, Timmers, H T Marc, Berger, Imre, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics
Přispěvatelé: 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), Laboratoire européen de biologie moléculaire - European Molecular Biology Laboratory (EMBL Grenoble), European Molecular Biology Laboratory [Grenoble] (EMBL), 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), 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), Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, 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)
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Models
Molecular
Transcription
Genetic
Protein subunit
genetic processes
information science
BrisSynBio
macromolecular substances
Crystallography
X-Ray
Article
Mass Spectrometry
03 medical and health sciences
0302 clinical medicine
Protein Domains
Structural Biology
Transcription (biology)
Humans
Molecular Biology
Transcription factor
ComputingMilieux_MISCELLANEOUS
TATA-Binding Protein Associated Factors
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
biology
General transcription factor
Chemistry
fungi
Bristol BioDesign Institute
TAF9
Cell biology
030104 developmental biology
Chaperone (protein)
Acetyltransferase
biology.protein
health occupations
Transcription Factor TFIID
Transcription factor II D
030217 neurology & neurosurgery
Chaperonin Containing TCP-1
HeLa Cells
Zdroj: Antonova, S V, Haffke, M, Corradini, E, Mikuciunas, M, Low, T Y, Signor, L, Van-Es, R M, Gupta, K, Scheer, E, Vos, H R, Tora, L, Heck, A J R, Timmers, H T M & Berger, I 2018, ' Chaperonin CCT Checkpoint Function in Basal Transcription Factor TFIID Assembly ', Nature Structural and Molecular Biology, vol. 25, no. 12, pp. 1119-1127 . https://doi.org/10.1038/s41594-018-0156-z
Nature structural & molecular biology
HAL
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2018, 25 (12), pp.1119-1127
Nature Structural and Molecular Biology, 25, 1119. Nature Publishing Group
Nature Structural and Molecular Biology, 2018, 25 (12), pp.1119-1127
ISSN: 1545-9993
1545-9985
Popis: TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit compositions exist and several TFIID subunits are shared with other complexes, thereby conveying precise cellular control of subunit allocation and functional assembly of this essential transcription factor. However, the molecular mechanisms that underlie the regulation of TFIID remain poorly understood. Here we use quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions that are crucial for TFIID integrity and for allocation of TAF9 to TFIID or the Spt-Ada-Gcn5 acetyltransferase (SAGA) co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are generated within the cell via mechanisms that involve checkpoint decisions facilitated by a chaperone.
Databáze: OpenAIRE
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