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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.
DNA primase small subunit is an enzyme that in humans is encoded by the PRIM1 gene. [ 5 ] 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 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.
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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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.