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Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase

Author

Listed:
  • Tomáš Kouba

    (EMBL Grenoble, 71 Avenue des Martyrs)

  • Tomáš Koval’

    (Centre BIOCEV, Průmyslová 595)

  • Petra Sudzinová

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Jiří Pospíšil

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Barbora Brezovská

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Jarmila Hnilicová

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Hana Šanderová

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Martina Janoušková

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Michaela Šiková

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Petr Halada

    (Institute of Microbiology of The Czech Academy of Sciences)

  • Michal Sýkora

    (Institute of Molecular Genetics of the Czech Academy of Sciences)

  • Ivan Barvík

    (Faculty of Mathematics and Physics, Institute of Physics, Charles University)

  • Jiří Nováček

    (CEITEC, Masaryk University)

  • Mária Trundová

    (Centre BIOCEV, Průmyslová 595)

  • Jarmila Dušková

    (Centre BIOCEV, Průmyslová 595)

  • Tereza Skálová

    (Centre BIOCEV, Průmyslová 595)

  • URee Chon

    (Pennsylvania State University)

  • Katsuhiko S. Murakami

    (Pennsylvania State University)

  • Jan Dohnálek

    (Centre BIOCEV, Průmyslová 595)

  • Libor Krásný

    (Institute of Microbiology of The Czech Academy of Sciences)

Abstract

RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.

Suggested Citation

  • Tomáš Kouba & Tomáš Koval’ & Petra Sudzinová & Jiří Pospíšil & Barbora Brezovská & Jarmila Hnilicová & Hana Šanderová & Martina Janoušková & Michaela Šiková & Petr Halada & Michal Sýkora & Ivan Barvík, 2020. "Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-20158-4
    DOI: 10.1038/s41467-020-20158-4
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    Cited by:

    1. Tomáš Kovaľ & Nabajyoti Borah & Petra Sudzinová & Barbora Brezovská & Hana Šanderová & Viola Vaňková Hausnerová & Alena Křenková & Martin Hubálek & Mária Trundová & Kristýna Adámková & Jarmila Dušková, 2024. "Mycobacterial HelD connects RNA polymerase recycling with transcription initiation," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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