IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-60484-z.html
   My bibliography  Save this article

Mechanism of DNA degradation by CBASS Cap5 endonuclease immune effector

Author

Listed:
  • Olga Rechkoblit

    (Icahn School of Medicine at Mount Sinai)

  • Daniela Sciaky

    (Icahn School of Medicine at Mount Sinai)

  • Mi Ni

    (Icahn School of Medicine at Mount Sinai)

  • Yangmei Li

    (Icahn School of Medicine at Mount Sinai)

  • Jithesh Kottur

    (Icahn School of Medicine at Mount Sinai
    Institute of Advanced Virology)

  • Gang Fang

    (Icahn School of Medicine at Mount Sinai)

  • Aneel K. Aggarwal

    (Icahn School of Medicine at Mount Sinai)

Abstract

Bacterial CBASS immune defense systems commonly kill virally infected cells by degrading genomic DNA in a form of cell suicide or abortive infection. We present a high-resolution structure of the CBASS effector Cap5, activated by a cyclic nucleotide, in the act of digesting DNA via tetrameric HNH endonuclease domains. Two HNH domains are in a catalytically active state for cleavage of the DNA strands, whereas the other two HNH domains are in a topologically distinct catalytically inactive state for simply DNA binding. The four HNH domains track one face of the DNA and mark an enzyme that acts as a stand-alone non-specific nuclease. We also show that chromosomally encoded CBASS Cap5 can be extrinsically activated by a cyclic nucleotide, as a step towards potential antibiotics.

Suggested Citation

  • Olga Rechkoblit & Daniela Sciaky & Mi Ni & Yangmei Li & Jithesh Kottur & Gang Fang & Aneel K. Aggarwal, 2025. "Mechanism of DNA degradation by CBASS Cap5 endonuclease immune effector," Nature Communications, Nature, vol. 16(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60484-z
    DOI: 10.1038/s41467-025-60484-z
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-60484-z
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-60484-z?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
    ---><---

    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:16:y:2025:i:1:d:10.1038_s41467-025-60484-z. 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.