IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v412y2001i6847d10.1038_35088000.html
   My bibliography  Save this article

Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair

Author

Listed:
  • John R. Walker

    (Cellular Biochemistry and Biophysics Program)

  • Richard A. Corpina

    (Cellular Biochemistry and Biophysics Program)

  • Jonathan Goldberg

    (Cellular Biochemistry and Biophysics Program
    Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center)

Abstract

The Ku heterodimer (Ku70 and Ku80 subunits) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. The crystal structure of the human Ku heterodimer was determined both alone and bound to a 55-nucleotide DNA element at 2.7 and 2.5 Å resolution, respectively. Ku70 and Ku80 share a common topology and form a dyad-symmetrical molecule with a preformed ring that encircles duplex DNA. The binding site can cradle two full turns of DNA while encircling only the central 3–4 base pairs (bp). Ku makes no contacts with DNA bases and few with the sugar-phosphate backbone, but it fits sterically to major and minor groove contours so as to position the DNA helix in a defined path through the protein ring. These features seem well designed to structurally support broken DNA ends and to bring the DNA helix into phase across the junction during end processing and ligation.

Suggested Citation

  • John R. Walker & Richard A. Corpina & Jonathan Goldberg, 2001. "Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair," Nature, Nature, vol. 412(6847), pages 607-614, August.
    • Handle: RePEc:nat:nature:v:412:y:2001:i:6847:d:10.1038_35088000
    DOI: 10.1038/35088000
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35088000
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35088000?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. Benjamin M. Stinson & Sean M. Carney & Johannes C. Walter & Joseph J. Loparo, 2024. "Structural role for DNA Ligase IV in promoting the fidelity of non-homologous end joining," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Ida Friis & Ilia A Solov’yov, 2018. "Activation of the DNA-repair mechanism through NBS1 and MRE11 diffusion," PLOS Computational Biology, Public Library of Science, vol. 14(7), pages 1-16, July.
    3. Jun Huang & David Rowe & Pratima Subedi & Wei Zhang & Tyler Suelter & Barbara Valent & David E. Cook, 2022. "CRISPR-Cas12a induced DNA double-strand breaks are repaired by multiple pathways with different mutation profiles in Magnaporthe oryzae," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    4. Zhen Shu & Bhakti Dwivedi & Jeffrey M. Switchenko & David S. Yu & Xingming Deng, 2024. "PD-L1 deglycosylation promotes its nuclear translocation and accelerates DNA double-strand-break repair in cancer," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    5. Angel Rivera-Calzada & Raquel Arribas-Bosacoma & Alba Ruiz-Ramos & Paloma Escudero-Bravo & Jasminka Boskovic & Rafael Fernandez-Leiro & Antony W. Oliver & Laurence H. Pearl & Oscar Llorca, 2022. "Structural basis for the inactivation of cytosolic DNA sensing by the vaccinia virus," Nature Communications, Nature, vol. 13(1), pages 1-13, 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:412:y:2001:i:6847:d:10.1038_35088000. 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.