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Cas9 (CRISPR associated protein 9, formerly called Cas5, Csn1, or Csx12) is a 160 kilodalton protein which plays a vital role in the immunological defense of certain bacteria against DNA viruses and plasmids, and is heavily utilized in genetic engineering applications.
CRISPR-associated transposons are similar to the Tn7 transposon which functions with a cut and paste mechanism. [1] It contains a heteromeric transposase consisting of TnsA and TnsB proteins, and a regulator protein TnsC. [1]
But Cas9 will not cleave the protospacer sequence unless there is an adjacent PAM sequence. The spacer in the bacterial CRISPR loci will not contain a PAM sequence, and thus will not be cut by the nuclease, but the protospacer in the invading virus or plasmid will contain the PAM sequence, and thus will be cleaved by the Cas9 nuclease. [4]
In the I-E system of E. coli, Cas1 and Cas2 form a complex where a Cas2 dimer bridges two Cas1 dimers. [116] In this complex, Cas2 performs a non-enzymatic scaffolding role, [ 116 ] binding double-stranded fragments of invading DNA, while Cas1 binds the single-stranded flanks of the DNA and catalyses their integration into CRISPR arrays.
Cas1 is a metal-dependent DNA-specific endonuclease that produces double-stranded DNA fragments. [1] Cas1 forms a stable complex with the other universally conserved CRISPR-associated protein, cas2 , which is essential to spacer acquisition for CRISPR systems.
This representation allows global visualization of different categories of events following Cas9-, D10A-, and H840-dependent cleavage in wATG− CR+/y+ wATG+ CS1− individuals. Nickases are more effective at producing HTR than Cas9, with H840 inducing the highest levels of conversion.