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• W2765660648 abstract "CRISPR-Cas systems confer an adaptive immunity against viruses. Following viral injection, Cas1-Cas2 integrates segments of the viral genome (spacers) into the CRISPR locus. In type I CRISPR-Cas systems, efficient primed spacer acquisition and viral degradation (interference) require both the Cascade complex and the Cas3 helicase/nuclease. Here, we present single-molecule characterization of the Thermobifida fusca (Tfu) primed acquisition complex (PAC). We show that TfuCascade rapidly samples non-specific DNA via facilitated one-dimensional diffusion. Cas3 loads at target-bound Cascade and the Cascade/Cas3 complex translocates via a looped DNA intermediate. Cascade/Cas3 complexes stall at diverse protein roadblocks, resulting in a double strand break at the stall site. In contrast, Cas1-Cas2 samples DNA transiently via 3D collisions. Moreover, Cas1-Cas2 associates with Cascade and translocates with Cascade/Cas3, forming the PAC. PACs can displace different protein roadblocks, suggesting a mechanism for long-range spacer acquisition. This work provides a molecular basis for the coordinated steps in CRISPR-based adaptive immunity." @default.
• W2765660648 created "2017-11-10" @default.
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• W2765660648 date "2018-11-01" @default.
• W2765660648 modified "2023-10-09" @default.
• W2765660648 title "Assembly and Translocation of a CRISPR-Cas Primed Acquisition Complex" @default.
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• W2765660648 doi "https://doi.org/10.1016/j.cell.2018.09.039" @default.
• W2765660648 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6441324" @default.
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• W2765660648 hasPublicationYear "2018" @default.
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