IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v469y2011i7331d10.1038_nature09688.html
   My bibliography  Save this article

Structural basis for site-specific ribose methylation by box C/D RNA protein complexes

Author

Listed:
  • Jinzhong Lin

    (National Institute of Biological Sciences)

  • Shaomei Lai

    (National Institute of Biological Sciences)

  • Ru Jia

    (National Institute of Biological Sciences)

  • Anbi Xu

    (National Institute of Biological Sciences)

  • Liman Zhang

    (National Institute of Biological Sciences
    Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College)

  • Jing Lu

    (National Institute of Biological Sciences
    Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College)

  • Keqiong Ye

    (National Institute of Biological Sciences)

Abstract

Target recognition by a guide RNA Some RNAs, called guide RNAs, use their encoded sequence information to help direct a protein to where it is required. One of these RNA-protein (RNP) complexes, known as the box C/D RNP, catalyses the site-specific modification of RNAs with a 2′-O-methylation group. The structure of the full box C/D RNP complex, including three protein subunits, the guide RNA and either of two substrate RNAs, has now been determined. The structure reveals how the guide and target RNAs are aligned, and how the methyltransferase subunit, fibrillarin, facilitates positioning of the target ribose into the active site.

Suggested Citation

  • Jinzhong Lin & Shaomei Lai & Ru Jia & Anbi Xu & Liman Zhang & Jing Lu & Keqiong Ye, 2011. "Structural basis for site-specific ribose methylation by box C/D RNA protein complexes," Nature, Nature, vol. 469(7331), pages 559-563, January.
  • Handle: RePEc:nat:nature:v:469:y:2011:i:7331:d:10.1038_nature09688
    DOI: 10.1038/nature09688
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09688
    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/nature09688?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:469:y:2011:i:7331:d:10.1038_nature09688. 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.