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

Roisin E. O’Brien, Inês C. Santos, Daniel Wrapp, Jack P. K. Bravo, Evan A. Schwartz, Jennifer S. Brodbelt and David W. Taylor ()
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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

Nature Communications, 2020, vol. 11, issue 1, 1-6

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-19785-8

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