ArticleRNA (New York, N.Y.)2016
The CRISPR-associated Csx1 protein of Pyrococcus furiosus is an adenosine-specific endoribonuclease.
Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 83 citations in OpenAlex.
- Structural mechanism of SAM-AMP and SAM-AMPNature communications · 2026Article
- From CRISPR-Cas to Argonautes: Defense systems of bacteria and archaea in the hydrothermal deep subsurface.ISME communications · 2026Article
- A phage-encoded anti-CRISPR protein co-opts host enolase to prevent type III CRISPR immunity.Nature microbiology · 2025Article
- Cap1 forms a cyclic tetra-adenylate-induced membrane pore during the type III-A CRISPR-Cas immune response.bioRxiv : the preprint server for biology · 2025Article
- CARF-dependent preferential RNA cleavage by Csm6 increases drug susceptibility of mycobacteria.Nucleic acids research · 2025Article
- Cat1 forms filament networks to degrade NADScience (New York, N.Y.) · 2025Article
- Nucleic acid recognition during prokaryotic immunity.Molecular cell · 2025Review
- Cas10 relieves host growth arrest to facilitate spacer retention during type III-A CRISPR-Cas immunity.Cell host & microbe · 2024Article
- Selective degradation of phage RNAs by the Csm6 ribonuclease provides robust type III CRISPR immunity in Streptococcus thermophilus.Nucleic acids research · 2024Article
- The Cas10 nuclease activity relieves host dormancy to facilitate spacer acquisition and retention during type III-A CRISPR immunity.bioRxiv : the preprint server for biology · 2024Article
- Type III CRISPR-Cas: beyond the Cas10 effector complex.Trends in biochemical sciences · 2024Review
- Molecular basis of stepwise cyclic tetra-adenylate cleavage by the type III CRISPR ring nuclease Crn1/Sso2081.Nucleic acids research · 2023Article
- The arms race between bacteria CBASS and bacteriophages.Frontiers in immunology · 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
- Different modes of spacer acquisition by the Staphylococcus epidermidis type III-A CRISPR-Cas system.Nucleic acids research · 2022Article
- Unique properties of spacer acquisition by the type III-A CRISPR-Cas system.Nucleic acids research · 2022Article
- Enzymatic properties of CARF-domain proteins inFrontiers in microbiology · 2022Article
- Cyclic Tetra-Adenylate (cABiomolecules · 2021Article
- Type III CRISPR-Cas Systems: Deciphering the Most Complex Prokaryotic Immune System.Biochemistry. Biokhimiia · 2021Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Prokaryotes are frequently exposed to potentially harmful invasive nucleic acids from phages, plasmids, and transposons. One method of defense is the CRISPR-Cas adaptive immune system. Diverse CRISPR-Cas systems form distinct ribonucleoprotein effector complexes that target and cleave invasive nucleic acids to provide immunity. The Type III-B Cmr effector complex has been found to target the RNA and DNA of the invader in the various bacterial and archaeal organisms where it has been characterized. Interestingly, the gene encoding the Csx1 protein is frequently located in close proximity to the Cmr1-6 genes in many genomes, implicating a role for Csx1 in Cmr function. However, evidence suggests that Csx1 is not a stably associated component of the Cmr effector complex, but is necessary for DNA silencing by the Cmr system in Sulfolobus islandicus. To investigate the function of the Csx1 protein, we characterized the activity of recombinant Pyrococcus furiosus Csx1 against various nucleic acid substrates. We show that Csx1 is a metal-independent, endoribonuclease that acts selectively on single-stranded RNA and cleaves specifically after adenosines. The RNA cleavage activity of Csx1 is dependent upon a conserved HEPN motif located within the C-terminal domain of the protein. This motif is also key for activity in other known ribonucleases. Collectively, the findings indicate that invader silencing by Type III-B CRISPR-Cas systems relies both on RNA and DNA nuclease activities from the Cmr effector complex as well as on the affiliated, trans-acting Csx1 endoribonuclease.
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