ArticleNucleic acids research2020
Fuse to defuse: a self-limiting ribonuclease-ring nuclease fusion for type III CRISPR defence.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Mechanistic basis for selective Csm6-2 activation by cyclic penta-adenylate in a type III CRISPR-Cas system.The EMBO journal · 2026Article
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Structure and mechanism of the broad spectrum CRISPR-associated ring nuclease Crn4.Nature communications · 2025Article
- The twist-and-squeeze activation of CARF-fused adenosine deaminase by cyclic oligoadenylates.The EMBO journal · 2025Article
- Diversity and abundance of ring nucleases in type III CRISPR-Cas loci.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- CARF-dependent preferential RNA cleavage by Csm6 increases drug susceptibility of mycobacteria.Nucleic acids research · 2025Article
- Article
- Exploring the diversity of anti-defense systems across prokaryotes, phages and mobile genetic elements.Nucleic acids research · 2025Article
- Nucleotide Immune Signaling in CBASS, Pycsar, Thoeris, and CRISPR Antiphage Defense.Annual review of microbiology · 2024Review
- Exploring the diversity of anti-defense systems across prokaryotes, phages, and mobile genetic elements.bioRxiv : the preprint server for biology · 2024Article
- Structural insight into the Csx1-Crn2 fusion self-limiting ribonuclease of type III CRISPR system.Nucleic acids research · 2024Article
- Molecular mechanism of allosteric activation of the CRISPR ribonuclease Csm6 by cyclic tetra-adenylate.The EMBO journal · 2024Article
- Type III CRISPR-Cas: beyond the Cas10 effector complex.Trends in biochemical sciences · 2024Review
- Activation of Csm6 ribonuclease by cyclic nucleotide binding: in an emergency, twist to open.Nucleic acids research · 2023Article
- Putative nucleotide-based second messengers in archaea.microLife · 2023Review
- The diverse arsenal of type III CRISPR-Cas-associated CARF and SAVED effectors.Biochemical Society transactions · 2022Review
- Inactivation of Target RNA Cleavage of a III-B CRISPR-Cas System Induces Robust Autoimmunity inInternational journal of molecular sciences · 2022Article
- The CRISPR ancillary effector Can2 is a dual-specificity nuclease potentiating type III CRISPR defence.Nucleic acids research · 2021Article
- Controlling and enhancing CRISPR systems.Nature chemical biology · 2021Review
- Heavily Armed Ancestors: CRISPR Immunity and Applications in Archaea with a Comparative Analysis of CRISPR Types in Sulfolobales.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Type III CRISPR systems synthesise cyclic oligoadenylate (cOA) second messengers in response to viral infection of bacteria and archaea, potentiating an immune response by binding and activating ancillary effector nucleases such as Csx1. As these effectors are not specific for invading nucleic acids, a prolonged activation can result in cell dormancy or death. Some archaeal species encode a specialised ring nuclease enzyme (Crn1) to degrade cyclic tetra-adenylate (cA4) and deactivate the ancillary nucleases. Some archaeal viruses and bacteriophage encode a potent ring nuclease anti-CRISPR, AcrIII-1, to rapidly degrade cA4 and neutralise immunity. Homologues of this enzyme (named Crn2) exist in type III CRISPR systems but are uncharacterised. Here we describe an unusual fusion between cA4-activated CRISPR ribonuclease (Csx1) and a cA4-degrading ring nuclease (Crn2) from Marinitoga piezophila. The protein has two binding sites that compete for the cA4 ligand, a canonical cA4-activated ribonuclease activity in the Csx1 domain and a potent cA4 ring nuclease activity in the C-terminal Crn2 domain. The cA4 binding affinities and activities of the two constituent enzymes in the fusion protein may have evolved to ensure a robust but time-limited cOA-activated ribonuclease activity that is finely tuned to cA4 levels as a second messenger of infection.
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