Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)—assembles into a functional transcription fac...

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Published in:Nature communications 2015-01, Vol.6 (1), p.6011-6011, Article 6011
Main Authors: Trowitzsch, Simon, Viola, Cristina, Scheer, Elisabeth, Conic, Sascha, Chavant, Virginie, Fournier, Marjorie, Papai, Gabor, Ebong, Ima-Obong, Schaffitzel, Christiane, Zou, Juan, Haffke, Matthias, Rappsilber, Juri, Robinson, Carol V., Schultz, Patrick, Tora, Laszlo, Berger, Imre
Format: Article
Language:English
Subjects:
101/28
101/58
13/1
13/106
13/51
13/89
14/35
14/63
631/337/572
631/45/612/1229
631/45/612/822
631/80/389/2029
82/103
82/75
82/80
82/83
Amino Acid Motifs
Calorimetry
Cell Nucleus - metabolism
Crystallography, X-Ray
Cytoplasm - metabolism
HeLa Cells
Histones - chemistry
Humanities and Social Sciences
Humans
Life Sciences
Mass Spectrometry - methods
Models, Molecular
multidisciplinary
Protein Binding
Protein Multimerization
Protein Structure, Tertiary
Recombinant Proteins - metabolism
Science
Science (multidisciplinary)
Surface Plasmon Resonance
TATA-Binding Protein Associated Factors - metabolism
Transcription Factor TFIID - chemistry
Transcription Factor TFIID - metabolism
Transcription Factors - metabolism
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cited_by cdi_FETCH-LOGICAL-c542t-3b7f60d4f8260d6e436451be26a4991a0dbe73bef8d0e5959f3f5a2d51bbcb2e3
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container_end_page 6011
container_issue 1
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container_title Nature communications
container_volume 6
creator Trowitzsch, Simon
Viola, Cristina
Scheer, Elisabeth
Conic, Sascha
Chavant, Virginie
Fournier, Marjorie
Papai, Gabor
Ebong, Ima-Obong
Schaffitzel, Christiane
Zou, Juan
Haffke, Matthias
Rappsilber, Juri
Robinson, Carol V.
Schultz, Patrick
Tora, Laszlo
Berger, Imre
description General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)—assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8–TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core–TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo–TFIID, regulated by nuclear import of preformed cytoplasmic submodules. TFIID is an essential transcription factor complex that controls the expression of most protein-coding genes in eukaryotes. Here the authors identify and characterize a complex containing TAF2, TAF8 and TAF10, which assembles in the cytoplasm before integration into the nuclear holo–TFIID complex.
doi_str_mv 10.1038/ncomms7011
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aerospace journals</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest Health &amp; Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health &amp; Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied &amp; Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Trowitzsch, Simon</au><au>Viola, Cristina</au><au>Scheer, Elisabeth</au><au>Conic, Sascha</au><au>Chavant, Virginie</au><au>Fournier, Marjorie</au><au>Papai, Gabor</au><au>Ebong, Ima-Obong</au><au>Schaffitzel, Christiane</au><au>Zou, Juan</au><au>Haffke, Matthias</au><au>Rappsilber, Juri</au><au>Robinson, Carol V.</au><au>Schultz, Patrick</au><au>Tora, Laszlo</au><au>Berger, Imre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2015-01-14</date><risdate>2015</risdate><volume>6</volume><issue>1</issue><spage>6011</spage><epage>6011</epage><pages>6011-6011</pages><artnum>6011</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)—assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8–TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core–TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo–TFIID, regulated by nuclear import of preformed cytoplasmic submodules. TFIID is an essential transcription factor complex that controls the expression of most protein-coding genes in eukaryotes. Here the authors identify and characterize a complex containing TAF2, TAF8 and TAF10, which assembles in the cytoplasm before integration into the nuclear holo–TFIID complex.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>25586196</pmid><doi>10.1038/ncomms7011</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-7829-5505</orcidid><orcidid>https://orcid.org/0000-0002-2779-8679</orcidid><orcidid>https://orcid.org/0000-0001-7398-2250</orcidid><orcidid>https://orcid.org/0000-0001-7518-9045</orcidid><oa>free_for_read</oa></addata></record>
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identifier ISSN: 2041-1723
ispartof Nature communications, 2015-01, Vol.6 (1), p.6011-6011, Article 6011
issn 2041-1723
2041-1723
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4309443
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subjects 101/28
101/58
13/1
13/106
13/51
13/89
14/35
14/63
631/337/572
631/45/612/1229
631/45/612/822
631/80/389/2029
82/103
82/75
82/80
82/83
Amino Acid Motifs
Calorimetry
Cell Nucleus - metabolism
Crystallography, X-Ray
Cytoplasm - metabolism
HeLa Cells
Histones - chemistry
Humanities and Social Sciences
Humans
Life Sciences
Mass Spectrometry - methods
Models, Molecular
multidisciplinary
Protein Binding
Protein Multimerization
Protein Structure, Tertiary
Recombinant Proteins - metabolism
Science
Science (multidisciplinary)
Surface Plasmon Resonance
TATA-Binding Protein Associated Factors - metabolism
Transcription Factor TFIID - chemistry
Transcription Factor TFIID - metabolism
Transcription Factors - metabolism
title Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules
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