Oct 26, 2018

Structure reveals mechanism of CRISPR RNA-guided nuclease recruitment and anti-CRISPR viral mimicry

BioRxiv : the Preprint Server for Biology
MaryClare F RollinsBlake Wiedenheft

Abstract

Bacteria and archaea have evolved sophisticated adaptive immune systems that rely on CRISPR RNA (crRNA)-guided detection and nuclease-mediated elimination of invading nucleic acids. Here we present the cryo-EM structure of the type I-F CRISPR RNA-guided surveillance complex (Csy complex) from Pseudomonas aeruginosa bound to a double-stranded DNA target. Comparison of this structure to previously determined structures of this complex reveals a ~180-degree rotation of the C-terminal helical bundle on the "large" Cas8f subunit. We show that the dsDNA-induced conformational change in Cas8f exposes a Cas2/3 "nuclease recruitment helix" that is structurally homologous to a virally encoded anti-CRISPR protein (AcrIF3). Structural homology between Cas8f and AcrIF3 suggests that AcrIF3 is a mimic of the Cas8f nuclease recruitment helix, implying that cas genes may sometimes serve as genetic fodder for the evolution of anti-CRISPRs.

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Mentioned in this Paper

Immune System
Molecular Helix
Pseudomonas aeruginosa (antigen)
Carboxy-Terminal Amino Acid
Imaging Guided Therapy
Helix (Snails)
Archaea
Protein Subunits
Pharmacologic Substance
Pseudomonas aeruginosa

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