IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms7011.html
   My bibliography  Save this article

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

Author

Listed:
  • Simon Trowitzsch

    (European Molecular Biology Laboratory, Grenoble Outstation
    Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS)

  • Cristina Viola

    (European Molecular Biology Laboratory, Grenoble Outstation
    Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS)

  • Elisabeth Scheer

    (Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Sascha Conic

    (Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Virginie Chavant

    (Proteomics Platform, Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Marjorie Fournier

    (Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Gabor Papai

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Ima-Obong Ebong

    (Chemistry Research Laboratory, University of Oxford)

  • Christiane Schaffitzel

    (European Molecular Biology Laboratory, Grenoble Outstation
    Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS)

  • Juan Zou

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Matthias Haffke

    (European Molecular Biology Laboratory, Grenoble Outstation
    Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS)

  • Juri Rappsilber

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh
    Institute of Bioanalytics, Technische Universität Berlin)

  • Carol V. Robinson

    (Chemistry Research Laboratory, University of Oxford)

  • Patrick Schultz

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Laszlo Tora

    (Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire)

  • Imre Berger

    (European Molecular Biology Laboratory, Grenoble Outstation
    Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS
    School of Biochemistry, Bristol University)

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.

Suggested Citation

  • Simon Trowitzsch & Cristina Viola & Elisabeth Scheer & Sascha Conic & Virginie Chavant & Marjorie Fournier & Gabor Papai & Ima-Obong Ebong & Christiane Schaffitzel & Juan Zou & Matthias Haffke & Juri , 2015. "Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules," Nature Communications, Nature, vol. 6(1), pages 1-14, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7011
    DOI: 10.1038/ncomms7011
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms7011
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms7011?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7011. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.