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Type III CRISPR–Cas systems produce cyclic oligoadenylate second messengers

Niewoehner, Ole, Garcia-Doval, Carmela, Rostøl, Jakob T., Berk, Christian, Schwede, Frank, Bigler, Laurent, Hall, Jonathan, Marraffini, Luciano A., Jinek, Martin·2017·Nature
DOI 10.1038/nature23467

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Crossref · 10.1038/nature23467

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  • Csm6 is activated by cyclic oligoadenylates and has an auxiliary action by degrading foreign transcripts in a non-specific fashion.

    “Csm6 is activated by these oligoadenylates, and even though it is not a part of the Cascade effector complex, it has an auxiliary action by degrading foreign transcripts in a non-specific fashion [51,52].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [52]

    The Discussion (page unavailable) says cyclic oligoadenylates activate Csm6 and describes its additional role in targeting invader transcripts. The in vivo activity section reports degradation of phage transcripts by Csm6 and Csm3. The copy does not establish that Csm6 degrades those transcripts non-specifically, and it calls the relevant complex the type III interference complex, not Cascade. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Cas10 has a further role in activating non-specific RNase Csm6 by producing cyclic oligoadenylates from ATP molecules.

    “Recent studies also suggest that Cas10 has a further role in activating non-specific RNase Csm6, by producing cyclic oligoadenylates from ATP molecules.”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [52]

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Research works printed but not linked: 38

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Metadata

Authors
Niewoehner, O., Garcia-Doval, C., Rostøl, J. T., Berk, C., Schwede, F., Bigler, L., Hall, J., Marraffini, L. A., & Jinek, M.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2017-07-19
Volume
548
Issue
7669
Pages
543-548
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature23467
Cited by
509
References
3
Language
en
Licence
www.springer.com/tdm (tdm)

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