ArticleNucleic acids research2021
Structural basis for inhibition of the type I-F CRISPR-Cas surveillance complex by AcrIF4, AcrIF7 and AcrIF14.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- A phage DUF669 protein mediates post-cleavage DNA repair against host CRISPR immunity.Nature communications · 2026Article
- DefensePredictor: A machine learning model to discover prokaryotic immune systems.Science (New York, N.Y.) · 2026Article
- Review
- The anti-CRISPR protein AcrIE8.1 inhibits the type I-E CRISPR-Cas system by directly binding to the Cascade subunit Cas11.FEBS letters · 2026Article
- Research Progress on the Mechanism and Application of the Type I CRISPR-Cas System.International journal of molecular sciences · 2024Review
- A new anti-CRISPR gene promotes the spread of drug-resistance plasmids in Klebsiella pneumoniae.Nucleic acids research · 2024Article
- Article
- Insights into the inhibition of protospacer integration via direct interaction between Cas2 and AcrVA5.Nature communications · 2024Article
- Current Updates of CRISPR/Cas System and Anti-CRISPR Proteins: Innovative Applications to Improve the Genome Editing Strategies.International journal of nanomedicine · 2024Review
- Targeted elimination of Vancomycin resistance gene vanA by CRISPR-Cas9 system.BMC microbiology · 2023Article
- Structural and functional investigation of GajB protein in Gabija anti-phage defense.Nucleic acids research · 2023Article
- Elimination of blaBMC microbiology · 2023Article
- Article
- Distribution and molecular evolution of the anti-CRISPR family AcrIF7.PLoS biology · 2023Article
- Unveil the Secret of the Bacteria and Phage Arms Race.International journal of molecular sciences · 2023Review
- Structural basis of AcrIF24 as an anti-CRISPR protein and transcriptional suppressor.Nature chemical biology · 2022Article
- Molecular basis of dual anti-CRISPR and auto-regulatory functions of AcrIF24.Nucleic acids research · 2022Article
- Disarming of type I-F CRISPR-Cas surveillance complex by anti-CRISPR proteins AcrIF6 and AcrIF9.Scientific reports · 2022Article
- AcrIF5 specifically targets DNA-bound CRISPR-Cas surveillance complex for inhibition.Nature chemical biology · 2022Article
- Insights into the inhibition of type I-F CRISPR-Cas system by a multifunctional anti-CRISPR protein AcrIF24.Nature communications · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
CRISPR-Cas systems are adaptive immune systems in bacteria and archaea to defend against mobile genetic elements (MGEs) and have been repurposed as genome editing tools. Anti-CRISPR (Acr) proteins are produced by MGEs to counteract CRISPR-Cas systems and can be used to regulate genome editing by CRISPR techniques. Here, we report the cryo-EM structures of three type I-F Acr proteins, AcrIF4, AcrIF7 and AcrIF14, bound to the type I-F CRISPR-Cas surveillance complex (the Csy complex) from Pseudomonas aeruginosa. AcrIF4 binds to an unprecedented site on the C-terminal helical bundle of Cas8f subunit, precluding conformational changes required for activation of the Csy complex. AcrIF7 mimics the PAM duplex of target DNA and is bound to the N-terminal DNA vise of Cas8f. Two copies of AcrIF14 bind to the thumb domains of Cas7.4f and Cas7.6f, preventing hybridization between target DNA and the crRNA. Our results reveal structural detail of three AcrIF proteins, each binding to a different site on the Csy complex for inhibiting degradation of MGEs.
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Registered trials
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.