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Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis

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  • Adelaine K. W. Leung

    (MRC Laboratory of Molecular Biology, Hills Road
    Present address: Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, Massachusetts 02115, USA.)

  • Kiyoshi Nagai

    (MRC Laboratory of Molecular Biology, Hills Road)

  • Jade Li

    (MRC Laboratory of Molecular Biology, Hills Road)

Abstract

At the core of the spliceosome The complex that excises introns from pre-messenger RNAs, the spliceosome, is composed of ribonucleoprotein subcomplexes, or snRNPs. Most snRNPs contain a core unit of seven Sm proteins, an SMN (survival of motor neurons) chaperone, and an snRNA specific to each snRNP. Leung et al. have solved the structure of the U4 snRNP core. Comparison with a lower-resolution U1 snRNP structure reveals how different snRNAs induce structural changes that permit association of accessory factors that distinguish the various snRNPs.

Suggested Citation

  • Adelaine K. W. Leung & Kiyoshi Nagai & Jade Li, 2011. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis," Nature, Nature, vol. 473(7348), pages 536-539, May.
    • Handle: RePEc:nat:nature:v:473:y:2011:i:7348:d:10.1038_nature09956
    DOI: 10.1038/nature09956
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    Cited by:

    1. 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.

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