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Type III CRISPR-Cas systems produce cyclic oligoadenylate second messengers.

Ole Niewoehner1, Carmela Garcia-Doval1, Jakob T Rostøl2

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Type III CRISPR-Cas systems use a cyclic oligoadenylate second messenger to activate the Csm6 RNase. This discovery reveals a novel regulatory mechanism for CRISPR interference, similar to innate immunity signaling.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Immunology

Background:

  • Type III CRISPR-Cas systems provide prokaryotic immunity against invasive genetic elements.
  • The Csm6 protein acts as a standalone RNase in type III CRISPR interference, but its activation mechanism was unknown.

Purpose of the Study:

  • To elucidate the mechanism by which Csm6 activity is regulated in type III CRISPR-Cas systems.
  • To identify the signaling pathway linking invader detection to Csm6 activation.

Main Methods:

  • Investigated Csm6 activation using biochemical assays and genetic manipulation of type III CRISPR-Cas components.
  • Analyzed the role of the Cas10 subunit and the CRISPR-associated Rossmann fold (CARF) domain in Csm6 regulation.
  • Utilized in vivo assays to assess the functional consequences of specific mutations.

Main Results:

  • Demonstrated that Csm6 is activated by a cyclic oligoadenylate second messenger produced by the type III interference complex.
  • Identified the Cas10 subunit as the producer of this second messenger upon target RNA binding.
  • Showed that the CARF domain of Csm6 binds the cyclic oligoadenylate, leading to allosteric activation.
  • Mutations in Cas10 and Csm6's CARF domain confirmed the importance of this signaling pathway.

Conclusions:

  • Uncovered an unprecedented mechanism for regulating CRISPR interference via a second messenger.
  • The Cas10-generated cyclic oligoadenylate allosterically activates Csm6, linking target recognition to RNA degradation.
  • This signaling pathway shares conceptual similarities with oligoadenylate signaling in mammalian innate immunity.