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- W4307046945 abstract "CRISPR-Cas9-mediated genome editing depends on PAM recognition to initiate DNA unwinding. PAM mutations can abolish Cas9 binding and prohibit editing. Here, we identified a Cas9 from the thermophile Alicyclobacillus tengchongensis for which the PAM interaction can be robustly regulated by DNA topology. AtCas9 has a relaxed PAM of N4CNNN and N4RNNA (R = A/G) and is able to bind but not cleave targets with mutated PAMs. When PAM-mutated DNA was in underwound topology, AtCas9 exhibited enhanced binding affinity and high cleavage activity. Mechanistically, AtCas9 has a unique loop motif, which docked into the DNA major groove, and this interaction can be regulated by DNA topology. More importantly, AtCas9 showed near-PAMless editing of supercoiled plasmid in E. coli. In mammalian cells, AtCas9 exhibited broad PAM preference to edit plasmid with up to 72% efficiency and effective base editing at four endogenous loci, representing a potentially powerful tool for near-PAMless editing." @default.
- W4307046945 created "2022-10-23" @default.
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- W4307046945 date "2022-11-01" @default.
- W4307046945 modified "2023-10-16" @default.
- W4307046945 title "DNA topology regulates PAM-Cas9 interaction and DNA unwinding to enable near-PAMless cleavage by thermophilic Cas9" @default.
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- W4307046945 doi "https://doi.org/10.1016/j.molcel.2022.09.032" @default.
- W4307046945 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36272409" @default.
- W4307046945 hasPublicationYear "2022" @default.
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