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Structure of the initiation-competent RNA polymerase I and its implication for transcription

Author

Listed:
  • Michael Pilsl

    (Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie)

  • Corinne Crucifix

    (IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
    CNRS/Strasbourg University)

  • Gabor Papai

    (IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
    CNRS/Strasbourg University)

  • Ferdinand Krupp

    (IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
    CNRS/Strasbourg University)

  • Robert Steinbauer

    (Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
    Present address: Sandoz GmbH, Biochemiestraße 10, 6250 Kundl, Austria.)

  • Joachim Griesenbeck

    (Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie)

  • Philipp Milkereit

    (Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie)

  • Herbert Tschochner

    (Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie)

  • Patrick Schultz

    (IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
    CNRS/Strasbourg University)

Abstract

Eukaryotic RNA polymerase I (Pol I) is specialized in rRNA gene transcription synthesizing up to 60% of cellular RNA. High level rRNA production relies on efficient binding of initiation factors to the rRNA gene promoter and recruitment of Pol I complexes containing initiation factor Rrn3. Here, we determine the cryo-EM structure of the Pol I-Rrn3 complex at 7.5 Å resolution, and compare it with Rrn3-free monomeric and dimeric Pol I. We observe that Rrn3 contacts the Pol I A43/A14 stalk and subunits A190 and AC40, that association re-organizes the Rrn3 interaction interface, thereby preventing Pol I dimerization; and Rrn3-bound and monomeric Pol I differ from the dimeric enzyme in cleft opening, and localization of the A12.2 C-terminus in the active centre. Our findings thus support a dual role for Rrn3 in transcription initiation to stabilize a monomeric initiation competent Pol I and to drive pre-initiation complex formation.

Suggested Citation

  • Michael Pilsl & Corinne Crucifix & Gabor Papai & Ferdinand Krupp & Robert Steinbauer & Joachim Griesenbeck & Philipp Milkereit & Herbert Tschochner & Patrick Schultz, 2016. "Structure of the initiation-competent RNA polymerase I and its implication for transcription," Nature Communications, Nature, vol. 7(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12126
    DOI: 10.1038/ncomms12126
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    Cited by:

    1. Zakia Morichaud & Stefano Trapani & Rishi K. Vishwakarma & Laurent Chaloin & Corinne Lionne & Joséphine Lai-Kee-Him & Patrick Bron & Konstantin Brodolin, 2023. "Structural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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