IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v614y2023i7947d10.1038_s41586-022-05658-1.html
   My bibliography  Save this article

Structural basis of Rho-dependent transcription termination

Author

Listed:
  • Vadim Molodtsov

    (Rutgers University)

  • Chengyuan Wang

    (Rutgers University)

  • Emre Firlar

    (Rutgers University)

  • Jason T. Kaelber

    (Rutgers University)

  • Richard H. Ebright

    (Rutgers University)

Abstract

Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription–translation-coupling quality control in Escherichia coli1–4. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho’s function.

Suggested Citation

  • Vadim Molodtsov & Chengyuan Wang & Emre Firlar & Jason T. Kaelber & Richard H. Ebright, 2023. "Structural basis of Rho-dependent transcription termination," Nature, Nature, vol. 614(7947), pages 367-374, February.
  • Handle: RePEc:nat:nature:v:614:y:2023:i:7947:d:10.1038_s41586-022-05658-1
    DOI: 10.1038/s41586-022-05658-1
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-022-05658-1
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/s41586-022-05658-1?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Emily Petroni & Caroline Esnault & Daniel Tetreault & Ryan K. Dale & Gisela Storz & Philip P. Adams, 2023. "Extensive diversity in RNA termination and regulation revealed by transcriptome mapping for the Lyme pathogen Borrelia burgdorferi," Nature Communications, Nature, vol. 14(1), pages 1-23, December.
    2. Jing Zhang & Shuo Zhang & Wei Zhou & Xiang Zhang & Guanjin Li & Ruoxuan Li & Xingyu Lin & Ziying Chen & Fang Liu & Pan Shen & Xiaogen Zhou & Yue Gao & Zhenguo Chen & Yanjie Chao & Chengyuan Wang, 2024. "A widely conserved protein Rof inhibits transcription termination factor Rho and promotes Salmonella virulence program," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Tatsuo Yanagisawa & Yuko Murayama & Haruhiko Ehara & Mie Goto & Mari Aoki & Shun-ichi Sekine, 2024. "Structural basis of eukaryotic transcription termination by the Rat1 exonuclease complex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

    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:nature:v:614:y:2023:i:7947:d:10.1038_s41586-022-05658-1. 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.