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• W2975604509 abstract "SUMMARY Bacterial CRISPR-Cas systems employ RNA-guided nucleases to destroy foreign DNA. Bacteriophages, in turn, have evolved diverse “anti-CRISPR” proteins (Acrs) to counteract acquired immunity. In Listeria monocytogenes , prophages encode 2-3 distinct anti-Cas9 proteins, with acrIIA1 always present; however, its mechanism is unknown. Here, we report that AcrIIA1 binds with high affinity to Cas9 via the catalytic HNH domain and, in Listeria , triggers Cas9 degradation. AcrIIA1 displays broad-spectrum inhibition of Type II-A and II-C Cas9s, including an additional highly-diverged Listeria Cas9. During lytic infection, AcrIIA1 is insufficient for rapid Cas9 inactivation, thus phages require an additional “partner” Acr that rapidly blocks Cas9-DNA-binding. The AcrIIA1 N-terminal domain (AcrIIA1 NTD ) is dispensable for anti-CRISPR activity; instead it is required for optimal phage replication through direct transcriptional repression of the anti-CRISPR locus. AcrIIA1 NTD is widespread amongst Firmicutes , can repress anti-CRISPR deployment by other phages, and has been co-opted by hosts potentially as an “anti-anti-CRISPR.” In summary, Listeria phages utilize narrow-spectrum inhibitors of DNA binding to rapidly inactivate Cas9 in lytic growth and the broad-spectrum AcrIIA1 to stimulate Cas9 degradation for protection of the Listeria genome in lysogeny." @default.
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• W2975604509 date "2019-09-30" @default.
• W2975604509 modified "2023-09-27" @default.
• W2975604509 title "<i>Listeria</i>phages induce Cas9 degradation to protect lysogenic genomes" @default.
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• W2975604509 doi "https://doi.org/10.1101/787200" @default.
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