ArticleCell research2019
Coupling of ssRNA cleavage with DNase activity in type III-A CRISPR-Csm revealed by cryo-EM and biochemistry.
Article in Cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- A phage-encoded anti-CRISPR protein co-opts host enolase to prevent type III CRISPR immunity.Nature microbiology · 2025Article
- Cas7 meets Cas14: a strategic partnership in the type VII CRISPR-Cas.Protein & cell · 2025Article
- A naked-eye biosensing system based on one-pot RPA-CRISPR/Cas12a driver G4-hemin self-assembly forFrontiers in chemistry · 2025Article
- The rise and future of CRISPR-based approaches for high-throughput genomics.FEMS microbiology reviews · 2024Review
- Precise transcript targeting by CRISPR-Csm complexes.Nature biotechnology · 2023Article
- Cryo-EM structure and protease activity of the type III-E CRISPR-Cas effector.Nature microbiology · 2023Article
- Structure of theCurrent research in structural biology · 2023Article
- Article
- Target RNA-guided protease activity in type III-E CRISPR-Cas system.Nucleic acids research · 2022Article
- Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase.Nature communications · 2022Article
- Craspase is a CRISPR RNA-guided, RNA-activated protease.Science (New York, N.Y.) · 2022Article
- Structures of an active type III-A CRISPR effector complex.Structure (London, England : 1993) · 2022Article
- Type III CRISPR-based RNA editing for programmable control of SARS-CoV-2 and human coronaviruses.Nucleic acids research · 2022Article
- Structural and biochemical characterization of in vivo assembled Lactococcus lactis CRISPR-Csm complex.Communications biology · 2022Article
- Exploration ofChemical physics · 2021Article
- Structure-based functional mechanisms and biotechnology applications of anti-CRISPR proteins.Nature reviews. Molecular cell biology · 2021Review
- Regulation of the RNA and DNA nuclease activities required for Pyrococcus furiosus Type III-B CRISPR-Cas immunity.Nucleic acids research · 2020Article
- Inhibition mechanisms of AcrF9, AcrF8, and AcrF6 against type I-F CRISPR-Cas complex revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Characterization of a novel type III CRISPR-Cas effector provides new insights into the allosteric activation and suppression of the Cas10 DNase.Cell discovery · 2020Article
- Second Messenger cAMolecular cell · 2019Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The type III CRISPR-Cas (clustered regularly interspaced short palindromic repeats-CRISPR-associated genes) systems are bacterially encoded adaptive immune systems for defense against invading nucleic acids. They accomplish this task through the coordinated cleavage of invading substrates of single-stranded RNA and DNA (ssDNA and ssRNA) by the Csm (type III-A) or Cmr (type III-B) effector complexes. The ssRNA is complementarily bound to the CRISPR RNA (crRNA). However, the structural basis for the DNase and RNase activation of the Csm nucleoprotein complex is largely unknown. Here we report cryo-EM structures of the Csm-crRNA complex, with or without target ssRNA, at near-atomic resolution. Our cryo-EM maps allow us to build atomic models of the key macromolecular components, including Cas10, Csm2, Csm3, Csm4, crRNA and the invading ssRNA. Our structure resolves unambiguously the stoichiometry and tertiary structures of the Csm protein complex and the interactions between protein components and the crRNA/ssRNA. Interestingly, the new atomic structures of the Csm proteins presented here are similar to those of previously known Csm proteins in other species despite their low sequence similarity. Our combined structural and biochemical data suggest that ssRNA cleavage is preferentially carried out near its 5'-end, that the extent of interactions among the ssRNA, crRNA and the protein components regulates the DNase activity of the Csm complex, and that the 3' flanking sequence of ssRNA activates the Cas10 DNase activity allosterically.
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Registered trials
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