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Autor(en) / Beteiligte
Titel
Structure Reveals a Mechanism of CRISPR-RNA-Guided Nuclease Recruitment and Anti-CRISPR Viral Mimicry
Ist Teil von
  • Molecular cell, 2019-04, Vol.74 (1), p.132-142.e5
Ort / Verlag
United States: Elsevier Inc
Erscheinungsjahr
2019
Quelle
MEDLINE
Beschreibungen/Notizen
  • 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-electron microscopy (cryo-EM) structure of the type I-F crRNA-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 double-stranded DNA (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. [Display omitted] •Structure of the type I-F CRISPR-RNA-guided surveillance complex bound to dsDNA•R-loop formation drives a conformational change that signals nuclease recruitment•Viral anti-CRISPR is a mimic of the C-terminal helical bundle of Cas8f The structure of a CRISPR-RNA-guided surveillance complex bound to dsDNA reveals a viral immune suppressor protein (AcrIF3) that mimics a critical subunit of the surveillance complex, which helps explain the mechanism of nuclease recruitment for degradation of foreign DNA.

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