IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v499y2013i7456d10.1038_nature12242.html
   My bibliography  Save this article

Structural basis of histone H2A–H2B recognition by the essential chaperone FACT

Author

Listed:
  • Maria Hondele

    (Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
    Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Tobias Stuwe

    (Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    Present addresses: California Institute of Technology, Division of Chemistry and Chemical Engineering, 1200 East California Boulevard, Pasadena, California 91125, USA (T.S.); Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, California 94720-3204, USA (E.T.Z.).)

  • Markus Hassler

    (Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
    Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Felix Halbach

    (Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany)

  • Andrew Bowman

    (Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany)

  • Elisa T. Zhang

    (Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    Present addresses: California Institute of Technology, Division of Chemistry and Chemical Engineering, 1200 East California Boulevard, Pasadena, California 91125, USA (T.S.); Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, California 94720-3204, USA (E.T.Z.).)

  • Bianca Nijmeijer

    (Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Christiane Kotthoff

    (Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany)

  • Vladimir Rybin

    (Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany)

  • Stefan Amlacher

    (Biochemistry Center, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany)

  • Ed Hurt

    (Biochemistry Center, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany)

  • Andreas G. Ladurner

    (Butenandt Institute and LMU Biomedical Center, Faculty of Medicine, Ludwig Maximilians University of Munich, Butenandtstrasse 5, 81377 Munich, Germany
    Genome Biology Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
    Munich Cluster for Systems Neurology (SyNergy), 81377 Munich, Germany
    Center for Integrated Protein Science Munich (CIPSM), 81377 Munich, Germany)

Abstract

The crystal structure of the FACT histone chaperone domain Spt16M in complex with the H2A–H2B heterodimer is solved; Spt16M makes several interactions with histones and seems to block the interaction of H2B with DNA, which could explain how FACT destabilizes nucleosomes to promote transcription.

Suggested Citation

  • Maria Hondele & Tobias Stuwe & Markus Hassler & Felix Halbach & Andrew Bowman & Elisa T. Zhang & Bianca Nijmeijer & Christiane Kotthoff & Vladimir Rybin & Stefan Amlacher & Ed Hurt & Andreas G. Ladurn, 2013. "Structural basis of histone H2A–H2B recognition by the essential chaperone FACT," Nature, Nature, vol. 499(7456), pages 111-114, July.
    • Handle: RePEc:nat:nature:v:499:y:2013:i:7456:d:10.1038_nature12242
    DOI: 10.1038/nature12242
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12242
    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/nature12242?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:499:y:2013:i:7456:d:10.1038_nature12242. 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.