Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
dna polymerase alpha, dna polymerase beta, dna polymerase iii, pol beta, klenow fragment, dna polymerase delta, taq dna polymerase, pol delta, pol alpha, dna polymerase gamma, more
Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.
PabPolD might play an important role in DNA replication likely together with PabpolB, suggesting that archaea require two DNA polymerases at the replication fork
both DNA polymerase D and DNA polymerases B are DNA polymerizing enzymes exclusively. DNA polymerase D has a preference for a primed template. DNA polymerase D is a primer-directed DNA polymerase independently of the primer composition whereas DNA polymerase B behaves as an exclusively DNA primer-directed DNA polymerase. Proliferating cell nuclear antigen is required for DNA polymerases D to perform efficient DNA synthesis but not DNA polymerases B. DNA polymerase D, but not DNA polymerase B, contains strand displacement activity. In the presence of PabPCNA, however, both DNA polymerases D and B show strand displacement activity. Direct interaction between DNA polymerase D and proliferating cell nuclear antigen is DNA-dependent
PCR performance and fidelity parameters are highest in the presence of 20 mM Tris-HCl, pH 9.0, 1.5 mM MgSO4, 25 mM KCl, 10 mM (NH4)2SO4 and 40 microM of each dNTP. Under these conditions, the error rate is 0.66.10(-6) mutations/nucleotide/duplication
DNA polymerases PolB and PolD slip in vitro on a template that consists of single-stranded DNA (ssDNA) with a hairpin structure flanked by short direct repeats. Pyrococcus abyssi proliferating cell nuclear antigen increases replication fidelity of this template
PabPolD might play an important role in DNA replication likely together with PabpolB, suggesting that archaea require two DNA polymerases at the replication fork
varying magnesium concentration affects both slippage and overall DNA synthesisof DNA polymerase PolB and PolD. There is almost no synthesis by PolB, PolD or their exo-forms at low magnesium concentrations (0.10.5 mM). Synthesis is also inhibited at 1520 mM. Parental molecules are readily detectable together with heteroduplex molecules at low to medium magnesium concentrations (15 mM)
DNA polymerases have abortive DNA synthesis upon encountering apurinic/apyrimidinic sites. Under running start conditions, polB can incorporate in front of the damage and even replicate to the full-length oligonucleotides containing a specific apurinic/apyrimidinic site, but only when present at a molar excess. Conversely, bypassing activity of polD is strictly inhibited
the (G)-PYF box is located in a hydrophobic region close to the active site. The (G)-PYF box mutants exhibit altered DNA binding properties. In addition, the thermal stability of all mutants is reduced compared to that of wild type, and this effect could be attributed to increased exposure of the hydrophobic region