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A type III CRISPR ancillary ribonuclease degrades its cyclic oligoadenylate activator
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dc.contributor.author | Athukoralage, Januka S. | |
dc.contributor.author | Graham, Shirley | |
dc.contributor.author | Grüschow, Sabine | |
dc.contributor.author | Rouillon, Christophe | |
dc.contributor.author | White, Malcolm F. | |
dc.date.accessioned | 2019-07-01T15:30:02Z | |
dc.date.available | 2019-07-01T15:30:02Z | |
dc.date.issued | 2019-07-12 | |
dc.identifier.citation | Athukoralage , J S , Graham , S , Grüschow , S , Rouillon , C & White , M F 2019 , ' A type III CRISPR ancillary ribonuclease degrades its cyclic oligoadenylate activator ' , Journal of Molecular Biology , vol. 431 , no. 15 , pp. 2894-2899 . https://doi.org/10.1016/j.jmb.2019.04.041 | en |
dc.identifier.issn | 0022-2836 | |
dc.identifier.other | PURE: 258964689 | |
dc.identifier.other | PURE UUID: b6bb802a-ec5b-43de-a3de-3835f5458c10 | |
dc.identifier.other | RIS: urn:716FDBBBD6E7754E09AD75676AB8405A | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/57568115 | |
dc.identifier.other | Scopus: 85065895798 | |
dc.identifier.other | ORCID: /0000-0002-1666-0180/work/60427711 | |
dc.identifier.other | WOS: 000475997200019 | |
dc.identifier.uri | https://hdl.handle.net/10023/18017 | |
dc.description | This work was funded by a grant from the Biotechnology and Biological Sciences Research Council (Grant REF BB/S000313/1 to MFW). | en |
dc.description.abstract | Cyclic oligoadenylate (cOA) secondary messengers are generated by type III CRISPR systems in response to viral infection. cOA allosterically activates the CRISPR ancillary ribonucleases Csx1/Csm6, which degrade RNA non-specifically using a HEPN (Higher Eukaryotes and Prokaryotes, Nucleotide binding) active site. This provides effective immunity but can also lead to growth arrest in infected cells, necessitating a means to deactivate the ribonuclease once viral infection has been cleared. In the crenarchaea, dedicated ring nucleases degrade cA4 (cOA consisting of 4 AMP units), but the equivalent enzyme has not been identified in bacteria. We demonstrate that, in Thermus thermophilus HB8, the uncharacterized protein TTHB144 is a cA4-activated HEPN ribonuclease that also degrades its activator. TTHB144 binds and degrades cA4 at an N-terminal CARF (CRISPR-associated Rossman fold) domain. The two activities can be separated by site-directed mutagenesis. TTHB144 is thus the first example of a self-limiting CRISPR ribonuclease. | |
dc.language.iso | eng | |
dc.relation.ispartof | Journal of Molecular Biology | en |
dc.rights | © 2019 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | en |
dc.subject | CRISPR | en |
dc.subject | Anti-viral signaling | en |
dc.subject | Cyclic oligoadenylate | en |
dc.subject | Ring nuclease | en |
dc.subject | Thermus thermophilus | en |
dc.subject | QH301 Biology | en |
dc.subject | QR355 Virology | en |
dc.subject | NDAS | en |
dc.subject.lcc | QH301 | en |
dc.subject.lcc | QR355 | en |
dc.title | A type III CRISPR ancillary ribonuclease degrades its cyclic oligoadenylate activator | en |
dc.type | Journal article | en |
dc.contributor.sponsor | BBSRC | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1016/j.jmb.2019.04.041 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | BB/S000313/1 | en |
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