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Structural basis for the second step of group II intron splicing

Author

Listed:
  • Russell T. Chan

    (University of California, San Diego)

  • Jessica K. Peters

    (University of California, San Diego)

  • Aaron R. Robart

    (University of California, San Diego
    West Virginia University)

  • Timothy Wiryaman

    (University of California, San Diego)

  • Kanagalaghatta R. Rajashankar

    (Argonne National Laboratory)

  • Navtej Toor

    (University of California, San Diego)

Abstract

The group II intron and the spliceosome share a common active site architecture and are thought to be evolutionarily related. Here we report the 3.7 Å crystal structure of a eukaryotic group II intron in the lariat-3′ exon form, immediately preceding the second step of splicing, analogous to the spliceosomal P complex. This structure reveals the location of the intact 3′ splice site within the catalytic core of the group II intron. The 3′-OH of the 5′ exon is positioned in close proximity to the 3′ splice site for nucleophilic attack and exon ligation. The active site undergoes conformational rearrangements with the catalytic triplex having different configurations before and after the second step of splicing. We describe a complete model for the second step of group II intron splicing that incorporates a dynamic catalytic triplex being responsible for creating the binding pocket for 3′ splice site capture.

Suggested Citation

  • Russell T. Chan & Jessica K. Peters & Aaron R. Robart & Timothy Wiryaman & Kanagalaghatta R. Rajashankar & Navtej Toor, 2018. "Structural basis for the second step of group II intron splicing," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06678-0
    DOI: 10.1038/s41467-018-06678-0
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