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Structural basis for assembly of non-canonical small subunits into type I-C Cascade

Author

Listed:
  • Roisin E. O’Brien

    (University of Texas at Austin)

  • Inês C. Santos

    (University of Texas at Austin)

  • Daniel Wrapp

    (University of Texas at Austin)

  • Jack P. K. Bravo

    (University of Texas at Austin)

  • Evan A. Schwartz

    (University of Texas at Austin)

  • Jennifer S. Brodbelt

    (University of Texas at Austin)

  • David W. Taylor

    (University of Texas at Austin
    University of Texas at Austin
    University of Texas at Austin
    Dell Medical School)

Abstract

Bacteria and archaea employ CRISPR (clustered, regularly, interspaced, short palindromic repeats)-Cas (CRISPR-associated) systems as a type of adaptive immunity to target and degrade foreign nucleic acids. While a myriad of CRISPR-Cas systems have been identified to date, type I-C is one of the most commonly found subtypes in nature. Interestingly, the type I-C system employs a minimal Cascade effector complex, which encodes only three unique subunits in its operon. Here, we present a 3.1 Å resolution cryo-EM structure of the Desulfovibrio vulgaris type I-C Cascade, revealing the molecular mechanisms that underlie RNA-directed complex assembly. We demonstrate how this minimal Cascade utilizes previously overlooked, non-canonical small subunits to stabilize R-loop formation. Furthermore, we describe putative PAM and Cas3 binding sites. These findings provide the structural basis for harnessing the type I-C Cascade as a genome-engineering tool.

Suggested Citation

  • Roisin E. O’Brien & Inês C. Santos & Daniel Wrapp & Jack P. K. Bravo & Evan A. Schwartz & Jennifer S. Brodbelt & David W. Taylor, 2020. "Structural basis for assembly of non-canonical small subunits into type I-C Cascade," Nature Communications, Nature, vol. 11(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19785-8
    DOI: 10.1038/s41467-020-19785-8
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