27 Facts About DNA polymerase

DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA.

DNA polymerase adds nucleotides to the three prime -end of a DNA strand, one nucleotide at a time.

DNA polymerase II was discovered by Thomas Kornberg and Malcolm E Gefter in 1970 while further elucidating the role of Pol I in E coli DNA replication.

Main function of DNA polymerase is to synthesize DNA from deoxyribonucleotides, the building blocks of DNA.

The DNA polymerase copies are created by the pairing of nucleotides to bases present on each strand of the original DNA polymerase molecule.

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When synthesizing new DNA, DNA polymerase can add free nucleotides only to the 3' end of the newly forming strand.

Since DNA polymerase requires a free 3' OH group for initiation of synthesis, it can synthesize in only one direction by extending the 3' end of the preexisting nucleotide chain.

Function of DNA polymerase is not quite perfect, with the enzyme making about one mistake for every billion base pairs copied.

Mismatches in DNA polymerase base pairing can potentially result in dysfunctional proteins and could lead to cancer.

Relative to the shape of DNA polymerase's binding pocket, steric clashes occur between the purine and residues in the minor groove, and important van der Waals and electrostatic interactions are lost by the pyrimidine.

However, although the different mismatches result in different steric properties, DNA polymerase is still able to detect and differentiate them so uniformly and maintain fidelity in DNA replication.

DNA polymerase polymerization is critical for many mutagenesis processes and is widely employed in biotechnologies.

Once it is bound, a nonprocessive DNA polymerase adds nucleotides at a rate of one nucleotide per second.

Retroviruses encode an unusual DNA polymerase called reverse transcriptase, which is an RNA-dependent DNA polymerase .

Taq DNA polymerase is a heat-stable enzyme of this family that lacks proofreading ability.

DNA polymerase II is a family B polymerase encoded by the polB gene.

Pfu DNA polymerase is a heat-stable enzyme of this family found in the hyperthermophilic archaeon Pyrococcus furiosus.

In E coli, DNA polymerase IV is an error-prone DNA polymerase involved in non-targeted mutagenesis.

DNA polymerase V is a Y-family DNA polymerase that is involved in SOS response and translesion synthesis DNA repair mechanisms.

However, the involvement of more than one TLS polymerase working in succession to bypass a lesion has not yet been shown in E coli.

In 1998, the family D of DNA polymerase was discovered in Pyrococcus furiosus and Methanococcus jannaschii.

The importance of these polymerases is evidenced by the fact that gene encoding DNA polymerase ? is referred as XPV, because loss of this gene results in the disease Xeroderma Pigmentosum Variant.

Pol ? another B family DNA polymerase, is made of two subunits Rev3, the catalytic subunit, and Rev7, which increases the catalytic function of the DNA polymerase, and is involved in translesion synthesis.

Any mutation that leads to limited or non-functioning Pol ? has a significant effect on mtDNA polymerase and is the most common cause of autosomal inherited mitochondrial disorders.

However, DNA polymerase nu plays an active role in homology repair during cellular responses to crosslinks, fulfilling its role in a complex with helicase.

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Retroviruses encode an unusual DNA polymerase called reverse transcriptase, which is an RNA-dependent DNA polymerase that synthesizes DNA from a template of RNA.

The phage DNA polymerase has an exonuclease activity that acts in a 3' to 5' direction, and this activity is employed in the proofreading and editing of newly inserted bases.