Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 6, Pages 528-534Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2820
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Funding
- US National Science Foundation [1244557]
- US National Science Foundation Graduate Research Fellowships
- University of California, Berkeley Chancellor's Fellowship
- Howard Hughes Medical Institute Fellow of the Life Sciences Research Foundation
- Long-Term Postdoctoral Fellowship
- Human Frontier Science Program Organization
- Investigator of the Howard Hughes Medical Institute
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1244557] Funding Source: National Science Foundation
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The initial stage of CRISPR-Cas immunity involves the integration of foreign DNA spacer segments into the host genomic CRISPR locus. The nucleases Cas1 and Cas2 are the only proteins conserved among all CRISPR-Cas systems, yet the molecular functions of these proteins during immunity are unknown. Here we show that Cas1 and Cas2 from Escherichia coli form a stable complex that is essential for spacer acquisition and determine the 2.3-angstrom-resolution crystal structure of the Cas1-Cas2 complex. Mutations that perturb Cas1-Cas2 complex formation disrupt CRISPR DNA recognition and spacer acquisition in vivo. Active site mutants of Cas2, unlike those of Cas1, can still acquire new spacers, thus indicating a nonenzymatic role of Cas2 during immunity. These results reveal the universal roles of Cas1 and Cas2 and suggest a mechanism by which Cas1-Cas2 complexes specify sites of CRISPR spacer integration.
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