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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.
The PRISMA flow diagram, depicting the flow of information through the different phases of a systematic review. PRISMA (Preferred Reporting Items for Systematic Reviews and Meta-Analyses) is an evidence-based minimum set of items aimed at helping scientific authors to report a wide array of systematic reviews and meta-analyses, primarily used to assess the benefits and harms of a health care ...
The Pol α complex (pol α-DNA primase complex) consists of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Once primase has created the RNA primer, Pol α starts replication elongating the primer with ~20 nucleotides.
In molecular biology and biochemistry, processivity is an enzyme's ability to catalyze "consecutive reactions without releasing its substrate". [1]For example, processivity is the average number of nucleotides added by a polymerase enzyme, such as DNA polymerase, per association event with the template strand.
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