ArticleNucleic acids research2021
Anti-CRISPR AcrIF9 functions by inducing the CRISPR-Cas complex to bind DNA non-specifically.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- A phage DUF669 protein mediates post-cleavage DNA repair against host CRISPR immunity.Nature communications · 2026Article
- Multilayer regulation of CRISPR systems: integrating anti-CRISPR proteins, CRISPRi/a, and quorum sensing networks.Frontiers in cellular and infection microbiology · 2026Review
- Mechanism of Cas9 inhibition by AcrIIA11.Nucleic acids research · 2025Article
- Article
- Making the leap from technique to treatment - genetic engineering is paving the way for more efficient phage therapy.Biochemical Society transactions · 2024Review
- Article
- Characterization of an efficient CRISPR-iCas9 system in Yarrowia lipolytica for the biosynthesis of carotenoids.Applied microbiology and biotechnology · 2023Article
- Unveil the Secret of the Bacteria and Phage Arms Race.International journal of molecular sciences · 2023Review
- Mechanisms regulating the CRISPR-Cas systems.Frontiers in microbiology · 2023Review
- Structural basis of AcrIF24 as an anti-CRISPR protein and transcriptional suppressor.Nature chemical biology · 2022Article
- Anti-CRISPR proteins function through thermodynamic tuning and allosteric regulation of CRISPR RNA-guided surveillance complex.Nucleic acids research · 2022Article
- Disarming of type I-F CRISPR-Cas surveillance complex by anti-CRISPR proteins AcrIF6 and AcrIF9.Scientific reports · 2022Article
- Alternative functions of CRISPR-Cas systems in the evolutionary arms race.Nature reviews. Microbiology · 2022Review
- Insights into the inhibition of type I-F CRISPR-Cas system by a multifunctional anti-CRISPR protein AcrIF24.Nature communications · 2022Article
- Structural insights into the inactivation of the type I-F CRISPR-Cas system by anti-CRISPR proteins.RNA biology · 2021Review
- Insights into the dual functions of AcrIF14 during the inhibition of type I-F CRISPR-Cas surveillance complex.Nucleic acids research · 2021Article
- Structure-based functional mechanisms and biotechnology applications of anti-CRISPR proteins.Nature reviews. Molecular cell biology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Phages and other mobile genetic elements express anti-CRISPR proteins (Acrs) to protect their genomes from destruction by CRISPR-Cas systems. Acrs usually block the ability of CRISPR-Cas systems to bind or cleave their nucleic acid substrates. Here, we investigate an unusual Acr, AcrIF9, that induces a gain-of-function to a type I-F CRISPR-Cas (Csy) complex, causing it to bind strongly to DNA that lacks both a PAM sequence and sequence complementarity. We show that specific and non-specific dsDNA compete for the same site on the Csy:AcrIF9 complex with rapid exchange, but specific ssDNA appears to still bind through complementarity to the CRISPR RNA. Induction of non-specific DNA-binding is a shared property of diverse AcrIF9 homologues. Substitution of a conserved positively charged surface on AcrIF9 abrogated non-specific dsDNA-binding of the Csy:AcrIF9 complex, but specific dsDNA binding was maintained. AcrIF9 mutants with impaired non-specific dsDNA binding activity in vitro displayed a reduced ability to inhibit CRISPR-Cas activity in vivo. We conclude that misdirecting the CRISPR-Cas complex to bind non-specific DNA is a key component of the inhibitory mechanism of AcrIF9. This inhibitory mechanism is distinct from a previously characterized anti-CRISPR, AcrIF1, that sterically blocks DNA-binding, even though AcrIF1and AcrIF9 bind to the same site on the Csy complex.
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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.