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DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some living organisms [ 1 ] ) segment called a primer complementary to a ssDNA (single-stranded DNA) template.
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The E. Coli DnaG primase is a 581 residue monomeric protein with three functional domains, according to proteolysis studies. There is an N-terminal Zinc-binding domain (residues 1–110) where a zinc ion is tetrahedrally coordinated between one histidine and three cysteine residues, which plays a role in recognizing sequence specific DNA binding sites.
PrimPol was identified in a bioinformatic study and initially presumed to only have primase activity. [8] Subsequent in vitro and in vivo studies have shown it to have both primase and polymerase activities that both localise to the catalytic domain of PrimPol. [6] [7] [9] For that reason, this protein was assigned the name PrimPol.
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