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CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

Author

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  • Xueni Li

    (University of Colorado Denver Anschutz Medical Campus)

  • Shiheng Liu

    (Electron Imaging Center for Nanomachines University of California, Los Angeles (UCLA)
    Immunology, and Molecular Genetics, UCLA)

  • Jiansen Jiang

    (Electron Imaging Center for Nanomachines University of California, Los Angeles (UCLA)
    Immunology, and Molecular Genetics, UCLA)

  • Lingdi Zhang

    (University of Colorado Denver Anschutz Medical Campus)

  • Sara Espinosa

    (University of Colorado Denver Anschutz Medical Campus)

  • Ryan C. Hill

    (University of Colorado Denver Anschutz Medical Campus)

  • Kirk C. Hansen

    (University of Colorado Denver Anschutz Medical Campus)

  • Z. Hong Zhou

    (Electron Imaging Center for Nanomachines University of California, Los Angeles (UCLA)
    Immunology, and Molecular Genetics, UCLA)

  • Rui Zhao

    (University of Colorado Denver Anschutz Medical Campus)

Abstract

U1 snRNP plays a critical role in 5ʹ-splice site recognition and is a frequent target of alternative splicing factors. These factors transiently associate with human U1 snRNP and are not amenable for structural studies, while their Saccharomyces cerevisiae (yeast) homologs are stable components of U1 snRNP. Here, we report the cryoEM structure of yeast U1 snRNP at 3.6 Å resolution with atomic models for ten core proteins, nearly all essential domains of its RNA, and five stably associated auxiliary proteins. The foot-shaped yeast U1 snRNP contains a core in the “ball-and-toes” region architecturally similar to the human U1 snRNP. All auxiliary proteins are in the “arch-and-heel” region and connected to the core through the Prp42/Prp39 paralogs. Our demonstration that homodimeric human PrpF39 directly interacts with U1C-CTD, mirroring yeast Prp42/Prp39, supports yeast U1 snRNP as a model for understanding how transiently associated auxiliary proteins recruit human U1 snRNP in alternative splicing.

Suggested Citation

  • Xueni Li & Shiheng Liu & Jiansen Jiang & Lingdi Zhang & Sara Espinosa & Ryan C. Hill & Kirk C. Hansen & Z. Hong Zhou & Rui Zhao, 2017. "CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing," Nature Communications, Nature, vol. 8(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01241-9
    DOI: 10.1038/s41467-017-01241-9
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    Cited by:

    1. Santiago Martínez-Lumbreras & Lena K. Träger & Miriam M. Mulorz & Marco Payr & Varvara Dikaya & Clara Hipp & Julian König & Michael Sattler, 2024. "Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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