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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.
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.
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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Griep studies the proteins that synthesize DNA, namely primase and DnaB helicase. [1] Of these, most of his work concerns primase, the enzyme that initiates DNA synthesis during DNA replication. His goal is to discover the next generation of antibiotics by searching for inhibitors of bacterial primase. To help him do this, he seeks to ...
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Pritelivir is a member of the helicase-primase inhibitors (HPI), a novel class of direct-acting antiviral drugs acting specifically against HSV-1 and HSV-2. [ 14 ] [ 15 ] As the name suggests, the drugs act through inhibition of the viral helicase primase complex , encoded by the UL5 (helicase), UL8 (scaffold protein) and UL52 (primase) genes ...