IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v467y2010i7311d10.1038_nature09318.html
   My bibliography  Save this article

Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae

Author

Listed:
  • Hengyao Niu

    (Yale University School of Medicine)

  • Woo-Hyun Chung

    (Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Zhu Zhu

    (Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Youngho Kwon

    (Yale University School of Medicine)

  • Weixing Zhao

    (Yale University School of Medicine)

  • Peter Chi

    (Yale University School of Medicine)

  • Rohit Prakash

    (Yale University School of Medicine)

  • Changhyun Seong

    (Yale University School of Medicine)

  • Dongqing Liu

    (Yale University School of Medicine)

  • Lucy Lu

    (Yale University School of Medicine)

  • Grzegorz Ira

    (Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

  • Patrick Sung

    (Yale University School of Medicine)

Abstract

Priming DNA for repair When DNA damage introduces double-strand breaks, the ends formed must undergo processing to prepare them for repair. In related studies by the Sung and Kowalczykowski laboratories, this processing reaction has been replicated in vitro using yeast proteins. Processing minimally requires the activities of a helicase, a nuclease and a single-strand binding protein, although the reaction is enhanced by further addition of three factors that help target the core complex and enhance the unwinding activity.

Suggested Citation

  • Hengyao Niu & Woo-Hyun Chung & Zhu Zhu & Youngho Kwon & Weixing Zhao & Peter Chi & Rohit Prakash & Changhyun Seong & Dongqing Liu & Lucy Lu & Grzegorz Ira & Patrick Sung, 2010. "Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae," Nature, Nature, vol. 467(7311), pages 108-111, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7311:d:10.1038_nature09318
    DOI: 10.1038/nature09318
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09318
    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/nature09318?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. Lorenzo Galanti & Martina Peritore & Robert Gnügge & Elda Cannavo & Johannes Heipke & Maria Dilia Palumbieri & Barbara Steigenberger & Lorraine S. Symington & Petr Cejka & Boris Pfander, 2024. "Dbf4-dependent kinase promotes cell cycle controlled resection of DNA double-strand breaks and repair by homologous recombination," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Priya Kapoor-Vazirani & Sandip K. Rath & Xu Liu & Zhen Shu & Nicole E. Bowen & Yitong Chen & Ramona Haji-Seyed-Javadi & Waaqo Daddacha & Elizabeth V. Minten & Diana Danelia & Daniela Farchi & Duc M. D, 2022. "SAMHD1 deacetylation by SIRT1 promotes DNA end resection by facilitating DNA binding at double-strand breaks," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    3. Chaoyou Xue & Sameer J. Salunkhe & Nozomi Tomimatsu & Ajinkya S. Kawale & Youngho Kwon & Sandeep Burma & Patrick Sung & Eric C. Greene, 2022. "Bloom helicase mediates formation of large single–stranded DNA loops during DNA end processing," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    4. Ananya Acharya & Kristina Kasaciunaite & Martin Göse & Vera Kissling & Raphaël Guérois & Ralf Seidel & Petr Cejka, 2021. "Distinct RPA domains promote recruitment and the helicase-nuclease activities of Dna2," Nature Communications, Nature, vol. 12(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:nature:v:467:y:2010:i:7311:d:10.1038_nature09318. 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.