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Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities

Author

Listed:
  • Allison L. Didychuk

    (University of Wisconsin)

  • Eric J. Montemayor

    (University of Wisconsin
    University of Wisconsin)

  • Tucker J. Carrocci

    (University of Wisconsin)

  • Andrew T. DeLaitsch

    (University of Wisconsin)

  • Stefani E. Lucarelli

    (University of Wisconsin)

  • William M. Westler

    (University of Wisconsin-Madison)

  • David A. Brow

    (University of Wisconsin)

  • Aaron A. Hoskins

    (University of Wisconsin)

  • Samuel E. Butcher

    (University of Wisconsin
    University of Wisconsin-Madison)

Abstract

U6 small nuclear ribonucleoprotein (snRNP) biogenesis is essential for spliceosome assembly, but not well understood. Here, we report structures of the U6 RNA processing enzyme Usb1 from yeast and a substrate analog bound complex from humans. Unlike the human ortholog, we show that yeast Usb1 has cyclic phosphodiesterase activity that leaves a terminal 3′ phosphate which prevents overprocessing. Usb1 processing of U6 RNA dramatically alters its affinity for cognate RNA-binding proteins. We reconstitute the post-transcriptional assembly of yeast U6 snRNP in vitro, which occurs through a complex series of handoffs involving 10 proteins (Lhp1, Prp24, Usb1 and Lsm2–8) and anti-cooperative interactions between Prp24 and Lhp1. We propose a model for U6 snRNP assembly that explains how evolutionarily divergent and seemingly antagonistic proteins cooperate to protect and chaperone the nascent snRNA during its journey to the spliceosome.

Suggested Citation

  • Allison L. Didychuk & Eric J. Montemayor & Tucker J. Carrocci & Andrew T. DeLaitsch & Stefani E. Lucarelli & William M. Westler & David A. Brow & Aaron A. Hoskins & Samuel E. Butcher, 2017. "Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities," Nature Communications, Nature, vol. 8(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00484-w
    DOI: 10.1038/s41467-017-00484-w
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