ArticleProceedings of the National Academy of Sciences of the United States of America2014
Molecular insights into DNA interference by CRISPR-associated nuclease-helicase Cas3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.
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Who cites it
53 citing papers in PubMed, 1 synthesis or guideline pooled it, 100 citations in OpenAlex.
- CRISPR-Cas systems in combating antimicrobial resistance: which system to choose? A systematic review.World journal of microbiology & biotechnology · 2025Pooled it
- Recent advances in CRISPR/Cas12a-based biosensors for heavy metal analysis: a review of signal readout strategies and analytical performance.Analytical and bioanalytical chemistry · 2026Review
- CRISPR-cas systems in pharmacology: functional pharmacogenomics, drug screening, resistance, and therapeutic translation.Functional & integrative genomics · 2026Review
- CRISPR rewired: from adaptive immunity to a global virulence control network in Salmonella.World journal of microbiology & biotechnology · 2026Review
- CRISPR-Cas targeting inmicroLife · 2026Article
- Structures reveal how the Cas1-2/3 integrase captures, delivers, and integrates foreign DNA into CRISPR loci.Structure (London, England : 1993) · 2025Article
- Structural basis of Cas3 activation in type I-C CRISPR-Cas system.Nucleic acids research · 2024Article
- Repurposing Type I-A CRISPR-Cas3 for a robust diagnosis of human papillomavirus (HPV).Communications biology · 2024Article
- Taxonomic Distribution, Phylogenetic Relationship, and Domain Conservation of CRISPR-Associated Cas Proteins.Bioinformatics and biology insights · 2024Article
- Repurposing the atypical type I-G CRISPR system for bacterial genome engineering.Microbiology (Reading, England) · 2023Article
- Dynamic interplay between target search and recognition for a Type I CRISPR-Cas system.Nature communications · 2023Article
- Article
- Allosteric control of type I-A CRISPR-Cas3 complexes and establishment as effective nucleic acid detection and human genome editing tools.Molecular cell · 2022Article
- Metal Dependence and Functional Diversity of Type I Cas3 Nucleases.Biochemistry · 2022Article
- CRISPR Interference as a Tool to Repress Gene Expression in Haloferax volcanii.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Double nicking by RNA-directed Cascade-nCas3 for high-efficiency large-scale genome engineering.Open biology · 2022Article
- Type III CRISPR-Cas Systems: Deciphering the Most Complex Prokaryotic Immune System.Biochemistry. Biokhimiia · 2021Review
- Genome editing in mammalian cells using the CRISPR type I-D nuclease.Nucleic acids research · 2021Article
- Prespacers formed during primed adaptation associate with the Cas1-Cas2 adaptation complex and the Cas3 interference nuclease-helicase.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pan-Genome Analysis Reveals Host-Specific Functional Divergences inMicroorganisms · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mobile genetic elements in bacteria are neutralized by a system based on clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins. Type I CRISPR-Cas systems use a "Cascade" ribonucleoprotein complex to guide RNA specifically to complementary sequence in invader double-stranded DNA (dsDNA), a process called "interference." After target recognition by Cascade, formation of an R-loop triggers recruitment of a Cas3 nuclease-helicase, completing the interference process by destroying the invader dsDNA. To elucidate the molecular mechanism of CRISPR interference, we analyzed crystal structures of Cas3 from the bacterium Thermobaculum terrenum, with and without a bound ATP analog. The structures reveal a histidine-aspartate (HD)-type nuclease domain fused to superfamily-2 (SF2) helicase domains and a distinct C-terminal domain. Binding of ATP analog at the interface of the SF2 helicase RecA-like domains rearranges a motif V with implications for the enzyme mechanism. The HD-nucleolytic site contains two metal ions that are positioned at the end of a proposed nucleic acid-binding tunnel running through the SF2 helicase structure. This structural alignment suggests a mechanism for 3' to 5' nucleolytic processing of the displaced strand of invader DNA that is coordinated with ATP-dependent 3' to 5' translocation of Cas3 along DNA. In agreement with biochemical studies, the presented Cas3 structures reveal important mechanistic details on the neutralization of genetic invaders by type I CRISPR-Cas systems.
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