AI Article Synopsis
- CRISPR-Cas systems are immune defenses in bacteria that protect against viruses and genetic elements; certain viruses, like ICP1, also have their own CRISPR-Cas systems to fight back.* -
- The ICP1 virus's Cas8f protein is missing a crucial domain for DNA cleavage, which raised questions about how it manages to interfere with host defenses.* -
- Research uncovered that Cas1, typically involved in adaptation, also plays a key role in DNA targeting during the interference stage by linking other proteins to the DNA, providing new insights into phage CRISPR mechanisms.*
Article Abstract
Clustered regularly interspaced short palindromic repeats (CRISPR)-Cas systems are prokaryotic adaptive immune systems against invading phages and other mobile genetic elements. Notably, some phages, including the Vibrio cholerae-infecting ICP1 (International Center for Diarrheal Disease Research, Bangladesh cholera phage 1), harbor CRISPR-Cas systems to counteract host defenses. Nevertheless, ICP1 Cas8f lacks the helical bundle domain essential for recruitment of helicase-nuclease Cas2/3 during target DNA cleavage and how this system accomplishes the interference stage remains unknown. Here, we found that Cas1, a highly conserved component known to exclusively work in the adaptation stage, also mediates the interference stage through connecting Cas2/3 to the DNA-bound CRISPR-associated complex for antiviral defense (Cascade; CRISPR system yersinia, Csy) of the ICP1 CRISPR-Cas system. A series of structures of Csy, Csy-dsDNA (double-stranded DNA), Cas1-Cas2/3 and Csy-dsDNA-Cas1-Cas2/3 complexes reveal the whole process of Cas1-mediated target DNA cleavage by the ICP1 CRISPR-Cas system. Together, these data support an unprecedented model in which Cas1 mediates the interference stage in a phage-encoded CRISPR-Cas system and the study also sheds light on a unique model of primed adaptation.
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| http://dx.doi.org/10.1038/s41589-024-01659-5 | DOI Listing |
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