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Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS

Author

Listed:
  • Julia Nagy

    (Biophysics Institute, Ulm University)

  • Dina Grohmann

    (Institut für Physikalische und Theoretische Chemie—NanoBioSciences, Technische Universität Braunschweig)

  • Alan C.M. Cheung

    (Institute for Structural and Molecular Biology, University College London)

  • Sarah Schulz

    (Institut für Physikalische und Theoretische Chemie—NanoBioSciences, Technische Universität Braunschweig)

  • Katherine Smollett

    (Institute for Structural and Molecular Biology, University College London)

  • Finn Werner

    (Institute for Structural and Molecular Biology, University College London)

  • Jens Michaelis

    (Biophysics Institute, Ulm University)

Abstract

The molecular architecture of RNAP II-like transcription initiation complexes remains opaque due to its conformational flexibility and size. Here we report the three-dimensional architecture of the complete open complex (OC) composed of the promoter DNA, TATA box-binding protein (TBP), transcription factor B (TFB), transcription factor E (TFE) and the 12-subunit RNA polymerase (RNAP) from Methanocaldococcus jannaschii. By combining single-molecule Förster resonance energy transfer and the Bayesian parameter estimation-based Nano-Positioning System analysis, we model the entire archaeal OC, which elucidates the path of the non-template DNA (ntDNA) strand and interaction sites of the transcription factors with the RNAP. Compared with models of the eukaryotic OC, the TATA DNA region with TBP and TFB is positioned closer to the surface of the RNAP, likely providing the mechanism by which DNA melting can occur in a minimal factor configuration, without the dedicated translocase/helicase encoding factor TFIIH.

Suggested Citation

  • Julia Nagy & Dina Grohmann & Alan C.M. Cheung & Sarah Schulz & Katherine Smollett & Finn Werner & Jens Michaelis, 2015. "Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS," Nature Communications, Nature, vol. 6(1), pages 1-12, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7161
    DOI: 10.1038/ncomms7161
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