ArticleNucleic acids research2023
Molecular basis of stepwise cyclic tetra-adenylate cleavage by the type III CRISPR ring nuclease Crn1/Sso2081.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 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
- Structural plasticity enables broad cAn binding and dual activation of CRISPR-associated ribonuclease Cdn1.Nucleic acids research · 2026Article
- 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
- The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease.Nucleic acids research · 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
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyclic oligoadenylates (cOAs) act as second messengers of the type III CRISPR immunity system through activating the auxiliary nucleases for indiscriminate RNA degradation. The cOA-degrading nucleases (ring nucleases) provide an 'off-switch' regulation of the signaling, thereby preventing cell dormancy or cell death. Here, we describe the crystal structures of the founding member of CRISPR-associated ring nuclease 1 (Crn1) Sso2081 from Saccharolobus solfataricus, alone, bound to phosphate ions or cA4 in both pre-cleavage and cleavage intermediate states. These structures together with biochemical characterizations establish the molecular basis of cA4 recognition and catalysis by Sso2081. The conformational changes in the C-terminal helical insert upon the binding of phosphate ions or cA4 reveal a gate-locking mechanism for ligand binding. The critical residues and motifs identified in this study provide a new insight to distinguish between cOA-degrading and -nondegrading CARF domain-containing proteins.
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Registered trials
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