IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v536y2016i7614d10.1038_nature18951.html
   My bibliography  Save this article

The structural basis of modified nucleosome recognition by 53BP1

Author

Listed:
  • Marcus D. Wilson

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue)

  • Samir Benlekbir

    (Molecular Structure and Function Program, The Hospital for Sick Children Research Institute)

  • Amélie Fradet-Turcotte

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
    † Present address: Laval University Cancer Research Center, Oncology Axis-CHU de Québec Research Center, Hôtel-Dieu de Québec, Quebec City, Quebec G1R 2J6 Canada; and Centre Hospitalier Universitaire de Québec Research Center, Université Laval, Quebec City, Quebec G1R 2J6, Canada.)

  • Alana Sherker

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
    University of Toronto)

  • Jean-Philippe Julien

    (Molecular Structure and Function Program, The Hospital for Sick Children Research Institute
    University of Toronto
    University of Toronto)

  • Andrea McEwan

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue)

  • Sylvie M. Noordermeer

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue)

  • Frank Sicheri

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
    University of Toronto
    University of Toronto)

  • John L. Rubinstein

    (Molecular Structure and Function Program, The Hospital for Sick Children Research Institute
    University of Toronto
    University of Toronto)

  • Daniel Durocher

    (The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
    University of Toronto)

Abstract

A cryo-electron microscopy structure of the DNA damage repair protein 53BP1 bound to a nucleosome illuminates the way 53BP1 recognizes two types of histone modifications (a methyl group and a ubiquitin moiety), and provides insight into the highly specified recognition and recruitment of 53BP1 to modified chromatin.

Suggested Citation

  • Marcus D. Wilson & Samir Benlekbir & Amélie Fradet-Turcotte & Alana Sherker & Jean-Philippe Julien & Andrea McEwan & Sylvie M. Noordermeer & Frank Sicheri & John L. Rubinstein & Daniel Durocher, 2016. "The structural basis of modified nucleosome recognition by 53BP1," Nature, Nature, vol. 536(7614), pages 100-103, August.
    • Handle: RePEc:nat:nature:v:536:y:2016:i:7614:d:10.1038_nature18951
    DOI: 10.1038/nature18951
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature18951
    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/nature18951?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.

    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:536:y:2016:i:7614:d:10.1038_nature18951. 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.