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Tetramerisation of the CRISPR ring nuclease Crn3/Csx3 facilitates cyclic oligoadenylate cleavage

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Athukoralage_2020_eLife_Tetramerisation_CC.pdf (3.706Mb)
Date
20/07/2020
Author
Athukoralage, Januka Sahan
McQuarrie, Stuart John
Gruschow, Sabine
Graham, Shirley
Gloster, Tracey
White, Malcolm
Funder
BBSRC
BBSRC
The Wellcome Trust
Grant ID
BB/T004789/1
BB/S000313/1
Keywords
CRISPR
Csx3
Ring nuclease
Cyclic tetra-adenylate
CARF
QD Chemistry
QH301 Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)
Neuroscience(all)
DAS
BDC
R2C
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Abstract
Type III CRISPR systems detect foreign RNA and activate the cyclase domain of the Cas10 subunit, generating cyclic oligoadenylate (cOA) molecules that act as a second messenger to signal infection, activating nucleases that degrade the nucleic acid of both invader and host. This can lead to dormancy or cell death; to avoid this, cells need a way to remove cOA from the cell once a viral infection has been defeated. Enzymes specialised for this task are known as ring nucleases, but are limited in their distribution. Here, we demonstrate that the widespread CRISPR associated protein Csx3, previously described as an RNA deadenylase, is a ring nuclease that rapidly degrades cyclic tetra-adenylate (cA4). The enzyme has an unusual cooperative reaction mechanism involving an active site that spans the interface between two dimers, sandwiching the cA4 substrate. We propose the name Crn3 (CRISPR associated ring nuclease 3) for the Csx3 family.
Citation
Athukoralage , J S , McQuarrie , S J , Gruschow , S , Graham , S , Gloster , T & White , M 2020 , ' Tetramerisation of the CRISPR ring nuclease Crn3/Csx3 facilitates cyclic oligoadenylate cleavage ' , eLife , vol. 9 , e57627 . https://doi.org/10.7554/eLife.57627
Publication
eLife
Status
Peer reviewed
DOI
https://doi.org/10.7554/eLife.57627
ISSN
2050-084X
Type
Journal article
Rights
Copyright © 2020, Athukoralage et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Description
Funding Information: This work was supported by the Biotechnology and Biological Sciences Research Council (REF: BB/S000313/1 to MFW and BB/T004789/1 to MFW and TMG) and by Wellcome Trust Institutional Strategic Support Funding to MFW and TMG (REF: 204821/Z/16/Z).
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  • University of St Andrews Research
URL
http://www.scopus.com/inward/record.url?scp=85087872973&partnerID=8YFLogxK
URI
http://hdl.handle.net/10023/20311

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