IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v458y2009i7237d10.1038_nature07851.html
   My bibliography  Save this article

Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution

Author

Listed:
  • Daniel A. Pomeranz Krummel

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
    Present addresses: Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA (D.A.P.K.); Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115, USA (A.K.W.L.).)

  • Chris Oubridge

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Adelaine K. W. Leung

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
    Present addresses: Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA (D.A.P.K.); Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115, USA (A.K.W.L.).)

  • Jade Li

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

  • Kiyoshi Nagai

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

Abstract

Human spliceosomal U1 small nuclear ribonucleoprotein particles (snRNPs), which consist of U1 small nuclear RNA and ten proteins, recognize the 5′ splice site within precursor messenger RNAs and initiate the assembly of the spliceosome for intron excision. An electron density map of the functional core of U1 snRNP at 5.5 Å resolution has enabled us to build the RNA and, in conjunction with site-specific labelling of individual proteins, to place the seven Sm proteins, U1-C and U1-70K into the map. Here we present the detailed structure of a spliceosomal snRNP, revealing a hierarchical network of intricate interactions between subunits. A striking feature is the amino (N)-terminal polypeptide of U1-70K, which extends over a distance of 180 Å from its RNA binding domain, wraps around the core domain consisting of the seven Sm proteins and finally contacts U1-C, which is crucial for 5′-splice-site recognition. The structure of U1 snRNP provides insights into U1 snRNP assembly and suggests a possible mechanism of 5′-splice-site recognition.

Suggested Citation

  • Daniel A. Pomeranz Krummel & Chris Oubridge & Adelaine K. W. Leung & Jade Li & Kiyoshi Nagai, 2009. "Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution," Nature, Nature, vol. 458(7237), pages 475-480, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07851
    DOI: 10.1038/nature07851
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07851
    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/nature07851?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.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Sébastien Campagne & Daniel Jutzi & Florian Malard & Maja Matoga & Ksenija Romane & Miki Feldmuller & Martino Colombo & Marc-David Ruepp & Frédéric H-T. Allain, 2023. "Molecular basis of RNA-binding and autoregulation by the cancer-associated splicing factor RBM39," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Josef Pánek & Adriana Roithová & Nenad Radivojević & Michal Sýkora & Archana Bairavasundaram Prusty & Nicholas Huston & Han Wan & Anna Marie Pyle & Utz Fischer & David Staněk, 2023. "The SMN complex drives structural changes in human snRNAs to enable snRNP assembly," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

    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:458:y:2009:i:7237:d:10.1038_nature07851. 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.