ArticleNucleic acids research2018
A Type III-B Cmr effector complex catalyzes the synthesis of cyclic oligoadenylate second messengers by cooperative substrate binding.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 61 citations in OpenAlex.
- Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.Structure (London, England : 1993) · 2026Article
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- AcrIIIA1 is a protein-RNA anti-CRISPR complex that targets core Cas and accessory nucleases.Nucleic acids research · 2024Article
- Retention of the RNA ends provides the molecular memory for maintaining the activation of the Csm complex.Nucleic acids research · 2024Article
- Molecular mechanism of allosteric activation of the CRISPR ribonuclease Csm6 by cyclic tetra-adenylate.The EMBO journal · 2024Article
- The influence of the copy number of invader on the fate of bacterial host cells in the antiviral defense by CRISPR-Cas10 DNases.Engineering microbiology · 2023Article
- An archaeal virus-encoded anti-CRISPR protein inhibits type III-B immunity by inhibiting Cas RNP complex turnover.Nucleic acids research · 2023Article
- Life strategies for Aminicenantia in subseafloor oceanic crust.The ISME journal · 2023Article
- Harnessing the LdCsm RNA Detection Platform for Efficient microRNA Detection.International journal of molecular sciences · 2023Article
- Article
- Inactivation of Target RNA Cleavage of a III-B CRISPR-Cas System Induces Robust Autoimmunity inInternational journal of molecular sciences · 2022Article
- Development of clustered regularly interspaced short palindromic repeats/CRISPR-associated technology for potential clinical applications.World journal of clinical cases · 2022Review
- Type III CRISPR-Cas Systems: Deciphering the Most Complex Prokaryotic Immune System.Biochemistry. Biokhimiia · 2021Review
- A type III-A CRISPR-Cas system mediates co-transcriptional DNA cleavage at the transcriptional bubbles in close proximity to active effectors.Nucleic acids research · 2021Article
- CRISPR-Cas adaptive immune systems in Sulfolobales: genetic studies and molecular mechanisms.Science China. Life sciences · 2021Review
- Analysis of a photosynthetic cyanobacterium rich in internal membrane systems via gradient profiling by sequencing (Grad-seq).The Plant cell · 2021Article
- Expression, purification, and characterization of a membrane-associated cyclic oligo-adenylate degrader fromSTAR protocols · 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
- Chemistry of Class 1 CRISPR-Cas effectors: Binding, editing, and regulation.The Journal of biological chemistry · 2020Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, Type III-A CRISPR-Cas systems were found to catalyze the synthesis of cyclic oligoadenylates (cOAs), a second messenger that specifically activates Csm6, a Cas accessory RNase and confers antiviral defense in bacteria. To test if III-B CRISPR-Cas systems could mediate a similar CRISPR signaling pathway, the Sulfolobus islandicus Cmr-α ribonucleoprotein complex (Cmr-α-RNP) was purified from the native host and tested for cOA synthesis. We found that the system showed a robust production of cyclic tetra-adenylate (c-A4), and that c-A4 functions as a second messenger to activate the III-B-associated RNase Csx1 by binding to its CRISPR-associated Rossmann Fold domain. Investigation of the kinetics of cOA synthesis revealed that Cmr-α-RNP displayed positively cooperative binding to the adenosine triphosphate (ATP) substrate. Furthermore, mutagenesis of conserved domains in Cmr2α confirmed that, while Palm 2 hosts the active site of cOA synthesis, Palm 1 domain serves as the primary site in the enzyme-substrate interaction. Together, our data suggest that the two Palm domains cooperatively interact with ATP molecules to achieve a robust cOA synthesis by the III-B CRISPR-Cas system.
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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.