Structure and mechanism of a Type III CRISPR defence DNA nuclease activated by cyclic oligoadenylate.

ABSTRACT: The CRISPR system provides adaptive immunity against mobile genetic elements in prokaryotes. On binding invading RNA species, Type III CRISPR systems generate cyclic oligoadenylate (cOA) signalling molecules, potentiating a powerful immune response by activating downstream effector proteins, leading to viral clearance, cell dormancy or death. Here we describe the structure and mechanism of a cOA-activated CRISPR defence DNA endonuclease, CRISPR ancillary nuclease 1 (Can1). Can1 has a unique monomeric structure with two CRISPR associated Rossman fold (CARF) domains and two DNA nuclease-like domains. The crystal structure of the enzyme has been captured in the activated state, with a cyclic tetra-adenylate (cA₄) molecule bound at the core of the protein. cA₄ binding reo

SUBMITTER: McMahon SA 

PROVIDER: S-EPMC6981274 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature