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DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 gene. [ 5 ] [ 6 ] The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components.
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.
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.
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.
During DNA replication, the double helix is unwound and the complementary strands are separated by the enzyme DNA helicase, creating what is known as the DNA replication fork. Following this fork, DNA primase and DNA polymerase begin to act in order to create a new complementary strand.
[5] [6] [7] PrimPol is a eukaryotic protein with both DNA polymerase and DNA Primase activities involved in translesion DNA synthesis. It is the first eukaryotic protein to be identified with priming activity using deoxyribonucleotides. [6] [7] It is also the first protein identified in the mitochondria to have translesion DNA synthesis activities.