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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.
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DNA polymerase alpha, like DNA primase, contains iron-sulfur clusters, that are critical in electron transport that uses DNA itself to transfer electrons at very high speeds; this process is involved in detecting DNA damage, and may also be involved in a feedback between the primase complex and the DNA polymerase alpha.
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Along the DNA template, primase intersperses RNA primers that DNA polymerase uses to synthesize DNA from in the 5′→3′ direction. [1] Another example of primers being used to enable DNA synthesis is reverse transcription. Reverse transcriptase is an enzyme that uses a template strand of RNA to synthesize a complementary strand of DNA.
A helicase–primase complex (also helicase-primase, Hel/Prim, H-P or H/P) is a complex of enzymes including DNA helicase and DNA primase. A helicase-primase associated factor protein may also be present. [1] The complex is used by herpesviruses, in which it is responsible for lytic DNA virus replication.