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New cuts for CRISPR effectors

Nature Reviews Genetics volume 24, page 71 (2023)Cite this article

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Leveraging CRISPR-derived proteins for biological applications has largely focused on CRISPR-associated nucleases for cleaving DNA or RNA target sites, or catalytically deficient nuclease domains for recruiting other enzymatic activities to target sites. However, studies of the evolutionary diversity of CRISPR systems are revealing other enzymatic activities with potential applications. Two new studies in Science characterize a CRISPR-associated nuclease–protease system that can be leveraged as a programmable protease-based RNA sensor.

In the latest work, both Kato et al. and Strecker et al. confirmed that purified Cas7-11 and Csx29 proteins from Desulfonema ishimotonii form a complex and then searched for putative substrates of the Csx29 protease. As functionally related CRISPR components are often encoded at the same locus, both teams first tested protease activity towards proteins encoded immediately upstream of csx29–cas7-11. In the presence of a target RNA bound to the Cas7-11 crRNA, the Csx29 protease cleaved another protein, Csx30. Both teams carried out extensive structural analyses by cryo-electron microscopy to show how binding of the target RNA causes structural reorganization of the Cas7-11–Csx29 complex to make the Csx29 active site competent for proteolysis of Csx30.

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References

Original articles

  • Kato, K. et al. RNA-triggered protein cleavage and cell growth arrest by the type III-E CRISPR nuclease-protease. Science 378, 882–889 (2022)

    Article  CAS  Google Scholar 

  • Strecker, J. et al. RNA-activated protein cleavage with a CRISPR-associated endopeptidase. Science 378, 874–881 (2022)

    Article  CAS  Google Scholar 

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  1. Nature Reviews Genetics http://www.nature.com/nrg/

    Darren J. Burgess

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  1. Darren J. Burgess
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Correspondence to Darren J. Burgess.

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Burgess, D.J. New cuts for CRISPR effectors. Nat Rev Genet 24, 71 (2023). https://doi.org/10.1038/s41576-022-00570-w

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