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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.
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.
19075 Ensembl ENSG00000198056 ENSMUSG00000025395 UniProt P49642 P20664 RefSeq (mRNA) NM_000946 NM_008921 RefSeq (protein) NP_000937 NP_032947 Location (UCSC) Chr 12: 56.73 – 56.75 Mb Chr 10: 127.85 – 127.87 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA primase small subunit is an enzyme that in humans is encoded by the PRIM1 gene. The replication of DNA in eukaryotic cells ...
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.
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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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.
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