IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v624y2023i7992d10.1038_s41586-023-06746-6.html
   My bibliography  Save this article

Structural insights into intron catalysis and dynamics during splicing

Author

Listed:
  • Ling Xu

    (Howard Hughes Medical Institute
    Yale University)

  • Tianshuo Liu

    (Yale University)

  • Kevin Chung

    (Yale University)

  • Anna Marie Pyle

    (Howard Hughes Medical Institute
    Yale University
    Yale University)

Abstract

The group II intron ribonucleoprotein is an archetypal splicing system with numerous mechanistic parallels to the spliceosome, including excision of lariat introns1,2. Despite the importance of branching in RNA metabolism, structural understanding of this process has remained elusive. Here we present a comprehensive analysis of three single-particle cryogenic electron microscopy structures captured along the splicing pathway. They reveal the network of molecular interactions that specifies the branchpoint adenosine and positions key functional groups to catalyse lariat formation and coordinate exon ligation. The structures also reveal conformational rearrangements of the branch helix and the mechanism of splice site exchange that facilitate the transition from branching to ligation. These findings shed light on the evolution of splicing and highlight the conservation of structural components, catalytic mechanism and dynamical strategies retained through time in premessenger RNA splicing machines.

Suggested Citation

  • Ling Xu & Tianshuo Liu & Kevin Chung & Anna Marie Pyle, 2023. "Structural insights into intron catalysis and dynamics during splicing," Nature, Nature, vol. 624(7992), pages 682-688, December.
    • Handle: RePEc:nat:nature:v:624:y:2023:i:7992:d:10.1038_s41586-023-06746-6
    DOI: 10.1038/s41586-023-06746-6
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-023-06746-6
    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/s41586-023-06746-6?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:624:y:2023:i:7992:d:10.1038_s41586-023-06746-6. 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.