IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-38144-x.html
   My bibliography  Save this article

Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli

Author

Listed:
  • Alexander T. Duckworth

    (University of Wisconsin-Madison)

  • Peter L. Ducos

    (University of Wisconsin-Madison
    Morgridge Institute for Research)

  • Sarah D. McMillan

    (University of Wisconsin-Madison)

  • Kenneth A. Satyshur

    (University of Wisconsin-Madison)

  • Katelien H. Blumenthal

    (University of Wisconsin-Madison)

  • Haley R. Deorio

    (University of Wisconsin-Madison)

  • Joseph A. Larson

    (University of Wisconsin-Madison)

  • Steven J. Sandler

    (University of Massachusetts at Amherst)

  • Timothy Grant

    (University of Wisconsin-Madison
    Morgridge Institute for Research)

  • James L. Keck

    (University of Wisconsin-Madison)

Abstract

Bacterial replisomes often dissociate from replication forks before chromosomal replication is complete. To avoid the lethal consequences of such situations, bacteria have evolved replication restart pathways that reload replisomes onto prematurely terminated replication forks. To understand how the primary replication restart pathway in E. coli (PriA-PriB) selectively acts on replication forks, we determined the cryogenic-electron microscopy structure of a PriA/PriB/replication fork complex. Replication fork specificity arises from extensive PriA interactions with each arm of the branched DNA. These interactions reshape the PriA protein to create a pore encircling single-stranded lagging-strand DNA while also exposing a surface of PriA onto which PriB docks. Together with supporting biochemical and genetic studies, the structure reveals a switch-like mechanism for replication restart initiation in which restructuring of PriA directly couples replication fork recognition to PriA/PriB complex formation to ensure robust and high-fidelity replication re-initiation.

Suggested Citation

  • Alexander T. Duckworth & Peter L. Ducos & Sarah D. McMillan & Kenneth A. Satyshur & Katelien H. Blumenthal & Haley R. Deorio & Joseph A. Larson & Steven J. Sandler & Timothy Grant & James L. Keck, 2023. "Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38144-x
    DOI: 10.1038/s41467-023-38144-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-38144-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-023-38144-x?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
    ---><---

    References listed on IDEAS

    as
    1. Michael M. Cox & Myron F. Goodman & Kenneth N. Kreuzer & David J. Sherratt & Steven J. Sandler & Kenneth J. Marians, 2000. "The importance of repairing stalled replication forks," Nature, Nature, vol. 404(6773), pages 37-41, March.
    2. Christian J. Rudolph & Amy L. Upton & Anna Stockum & Conrad A. Nieduszynski & Robert G. Lloyd, 2013. "Avoiding chromosome pathology when replication forks collide," Nature, Nature, vol. 500(7464), pages 608-611, August.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Dean Huang & Anna E. Johnson & Brandon S. Sim & Teresa W. Lo & Houra Merrikh & Paul A. Wiggins, 2023. "The in vivo measurement of replication fork velocity and pausing by lag-time analysis," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Judith Oehler & Carl A. Morrow & Matthew C. Whitby, 2023. "Gene duplication and deletion caused by over-replication at a fork barrier," Nature Communications, Nature, vol. 14(1), pages 1-15, 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:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38144-x. 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.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with 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.