IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v2y2011i1d10.1038_ncomms1320.html
   My bibliography  Save this article

Structure and Scm3-mediated assembly of budding yeast centromeric nucleosomes

Author

Listed:
  • Mekonnen Lemma Dechassa

    (Colorado State University)

  • Katharina Wyns

    (Colorado State University)

  • Ming Li

    (Cornell University)

  • Michael A. Hall

    (Cornell University)

  • Michelle D. Wang

    (Cornell University
    Cornell University
    Howard Hughes Medical Institute, 4000 Jones Bridge Road)

  • Karolin Luger

    (Colorado State University
    Howard Hughes Medical Institute, 4000 Jones Bridge Road)

Abstract

Much controversy exists regarding the structural organization of the yeast centromeric nucleosome and the role of the nonhistone protein, Scm3, in its assembly and architecture. Here we show that the substitution of H3 with its centromeric variant Cse4 results in octameric nucleosomes that organize DNA in a left-handed superhelix. We demonstrate by single-molecule approaches, micrococcal nuclease digestion and small-angle X-ray scattering that Cse4-nucleosomes exhibit an open conformation with weakly bound terminal DNA segments. The Cse4-octamer does not preferentially form nucleosomes on its cognate centromeric DNA. We show that Scm3 functions as a Cse4-specific nucleosome assembly factor, and that the resulting octameric nucleosomes do not contain Scm3 as a stably bound component. Taken together, our data provide insights into the assembly and structural features of the budding yeast centromeric nucleosome.

Suggested Citation

  • Mekonnen Lemma Dechassa & Katharina Wyns & Ming Li & Michael A. Hall & Michelle D. Wang & Karolin Luger, 2011. "Structure and Scm3-mediated assembly of budding yeast centromeric nucleosomes," Nature Communications, Nature, vol. 2(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1320
    DOI: 10.1038/ncomms1320
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms1320
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms1320?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:2:y:2011:i:1:d:10.1038_ncomms1320. 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.