Journal
SCIENCE
Volume 351, Issue 6275, Pages 867-871Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aad8282
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Funding
- Direct For Biological Sciences [1244557] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [1244557] Funding Source: National Science Foundation
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [P01 GM051487, T32 GM066698] Funding Source: Medline
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Bacterial adaptive immunity and genome engineering involving the CRISPR (clustered regularly interspaced short palindromic repeats)-associated (Cas) protein Cas9 begin with RNA-guided DNA unwinding to form an RNA-DNA hybrid and a displaced DNA strand inside the protein. The role of this R-loop structure in positioning each DNA strand for cleavage by the two Cas9 nuclease domains is unknown. We determine molecular structures of the catalytically active Streptococcus pyogenes Cas9 R-loop that show the displaced DNA strand located near the RuvC nuclease domain active site. These protein-DNA interactions, in turn, position the HNH nuclease domain adjacent to the target DNA strand cleavage site in a conformation essential for concerted DNA cutting. Cas9 bends the DNA helix by 30 degrees, providing the structural distortion needed for R-loop formation.
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