Evidence map›Paper›PMID 33590098›Full record

ArticleNucleic acids research2021

The CRISPR ancillary effector Can2 is a dual-specificity nuclease potentiating type III CRISPR defence.

Wenlong Zhu, Stuart McQuarrie, Sabine Grüschow, Stephen A McMahon, Shirley Graham, Tracey M Gloster, Malcolm F White

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 83 citations in OpenAlex.

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  13. Diversity and abundance of ring nucleases in type III CRISPR-Cas loci.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  14. SAM-AMP lyases in type III CRISPR defence.Nucleic acids research · 2025
    Article
  15. Cat1 forms filament networks to degrade NADScience (New York, N.Y.) · 2025
    Article
  16. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Wenlong ZhuBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Stuart McQuarrieBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Sabine GrüschowBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Stephen A McMahonBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Shirley GrahamBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Tracey M GlosterBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
Malcolm F WhiteBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK.
University of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S000313/1Biotechnology and Biological Sciences Research Council BB/T004789/1Wellcome TrustWellcome Trust 204821/Z/16/Z
6 · The paper itself

Abstract

Cells and organisms have a wide range of mechanisms to defend against infection by viruses and other mobile genetic elements (MGE). Type III CRISPR systems detect foreign RNA and typically generate cyclic oligoadenylate (cOA) second messengers that bind to ancillary proteins with CARF (CRISPR associated Rossman fold) domains. This results in the activation of fused effector domains for antiviral defence. The best characterised CARF family effectors are the Csm6/Csx1 ribonucleases and DNA nickase Can1. Here we investigate a widely distributed CARF family effector with a nuclease domain, which we name Can2 (CRISPR ancillary nuclease 2). Can2 is activated by cyclic tetra-adenylate (cA4) and displays both DNase and RNase activity, providing effective immunity against plasmid transformation and bacteriophage infection in Escherichia coli. The structure of Can2 in complex with cA4 suggests a mechanism for the cA4-mediated activation of the enzyme, whereby an active site cleft is exposed on binding the activator. These findings extend our understanding of type III CRISPR cOA signalling and effector function.

Indexed as

CRISPR-Cas SystemsClustered Regularly Interspaced Short Palindromic RepeatsCRISPR-Associated ProteinsDeoxyribonuclease IDNAEnzyme ActivationEscherichia coliEubacterialesInterspersed Repetitive SequencesMetalsModels, MolecularProtein DomainsRibonucleasesCRISPR-Associated ProteinsDeoxyribonuclease IDNAMetalsRibonucleases

Identifiers

PMID33590098
PMCPMC7969007
OpenAlexW3131429738

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.