1. Biochemistry and Chemical Biology
  2. Chromosomes and Gene Expression
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Archaeal TFEα/β is a hybrid of TFIIE and the RNA polymerase III subcomplex hRPC62/39

  1. Fabian Blombach
  2. Enrico Salvadori
  3. Thomas Fouqueau
  4. Jun Yan
  5. Julia Reimann
  6. Carol Sheppard
  7. Katherine L Smollett
  8. Sonja V Albers
  9. Christopher WM Kay
  10. Konstantinos Thalassinos
  11. Finn Werner  Is a corresponding author
  1. University College London, United Kingdom
  2. Max Planck Institute for Terrestrial Microbiology, Germany
Research Article
  • Cited 36
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Cite this article as: eLife 2015;4:e08378 doi: 10.7554/eLife.08378

Abstract

Transcription initiation of archaeal RNA polymerase (RNAP) and eukaryotic RNAPII is assisted by conserved basal transcription factors. The eukaryotic transcription factor TFIIE consists of α and β subunits. Here we have identified and characterised the function of the TFIIEβ homologue in archaea that on the primary sequence level is related to the RNAPIII subunit hRPC39. Both archaeal TFEβ and hRPC39 harbour a cubane 4Fe-4S cluster, which is crucial for heterodimerization of TFEα/β and its engagement with the RNAP clamp. TFEα/β stabilises the preinitiation complex, enhances DNA melting, and stimulates abortive and productive transcription. These activities are strictly dependent on the β subunit and the promoter sequence. Our results suggest that archaeal TFEα/β is likely to represent the evolutionary ancestor of TFIIE-like factors in extant eukaryotes.

Article and author information

Author details

  1. Fabian Blombach

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  2. Enrico Salvadori

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  3. Thomas Fouqueau

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  4. Jun Yan

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  5. Julia Reimann

    Molecular Biology of Archaea Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  6. Carol Sheppard

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  7. Katherine L Smollett

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  8. Sonja V Albers

    Molecular Biology of Archaea Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  9. Christopher WM Kay

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  10. Konstantinos Thalassinos

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  11. Finn Werner

    Institute for Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom
    For correspondence
    f.werner@ucl.ac.uk
    Competing interests
    The authors declare that no competing interests exist.

Reviewing Editor

  1. Patrick Cramer, Max Planck Institute for Biophysical Chemistry, Germany

Publication history

  1. Received: April 28, 2015
  2. Accepted: June 11, 2015
  3. Accepted Manuscript published: June 12, 2015 (version 1)
  4. Version of Record published: July 8, 2015 (version 2)

Copyright

© 2015, Blombach et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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