In DNA amplification A
DNA polymerase was discovered in
P. furiosus that was thought to be unrelated to other known DNA polymerases, as no significant
sequence homology was found between its two proteins and those of other known DNA polymerases. This DNA polymerase has strong
3'-to-5' exonucleolytic activity and a template-primer preference which is characteristic of a replicative DNA polymerase, leading scientists to believe that this enzyme may be the replicative DNA polymerase of
P. furiosus. It has since been placed in the family B of polymerases, the same family as DNA polymerase II. Its structure, which appears quite typical for polymerase B, has been solved as well. Since the
enzymes of
P. furiosus are extremely thermostable, the
DNA polymerase from
P. furiosus (also known as
Pfu DNA polymerase) can be used in the
polymerase chain reaction (PCR) DNA amplification process. The PCR process must use a thermostable DNA polymerase for automated in vitro amplification, which was originally used
Taq DNA polymerase. However, since purified
Taq DNA polymerase lacks
exonuclease (proofreading) activity, it cannot excise mismatched
nucleotides. Researchers discovered in the early 1990s that the
Pfu DNA polymerase of
P. furiosus does possess a requisite
3’-to-5’ exonuclease activity allowing for the removal of errors. Subsequent tests utilizing
Pfu DNA polymerase in the PCR process revealed a more than tenfold improvement over the accuracy of using
Taq DNA polymerase.
In production of diols One practical application of
P. furiosus is in the production of
diols for various industrial processes. It may be possible to use the enzymes of
P. furiosus for applications in such industries as food, pharmaceuticals, and fine-chemicals in which
alcohol dehydrogenases are necessary in the production of enantio- and diastereomerically pure diols. Enzymes from hyperthermophiles such as
P. furiosus can perform well in laboratory processes because they are relatively resistant: they generally function well at high temperatures and high pressures, as well as in high concentrations of chemicals. In order to make naturally derived enzymes useful in the laboratory, it is often necessary to alter their genetic makeup. Otherwise, the naturally occurring enzymes may not be efficient in an artificially induced procedure. Although the enzymes of
P. furiosus function optimally at a high temperature, scientists may not necessarily want to carry out a procedure at . Consequently, in this case, the specific enzyme AdhA was taken from
P. furiosus and put through various mutations in a laboratory in order to obtain a suitable alcohol dehydrogenase for use in artificial processes. This allowed scientists to obtain a mutant enzyme that could function efficiently at lower temperatures and maintain productivity.
In plants The expression of a certain gene found in
P. furiosus in plants can also render them more durable by increasing their tolerance for heat. In response to environmental stresses such as heat exposure, plants produce
reactive oxygen species which can result in cell death. If these free radicals are removed, cell death can be delayed. Enzymes in plants called
superoxide dismutases remove
superoxide anion radicals from cells, but increasing the amount and activity of these enzymes is difficult and not the most efficient way to go about improving the durability of plants. By introducing the
superoxide reductases of
P. furiosus into plants, the levels of O2 can be rapidly reduced. Scientists tested this method using the
Arabidopsis thaliana plant. As a result of this procedure, cell death in plants occurs less often, therefore resulting in a reduction in the severity of responses to environmental stress. This enhances the survival of plants, making them more resistant to light, chemical, and heat stress. This study could potentially be used as a starting point to creating plants that could survive in more extreme climates on other planets such as Mars. By introducing more enzymes from extremophiles like
P. furiosus into other species of plants, it may be possible to create incredibly resistant species.
In researching amino acids By comparing
P. furiosus with a related species of archaea,
Pyrococcus abyssi, scientists have tried to determine the correlation between certain amino acids and affinity for certain pressures in different species.
P. furiosus is not
barophilic, while
P. abyssi is, meaning that it functions optimally at very high pressures. Using two hyperthermophilic species of archaea lessens the possibility of deviations having to do with temperature of the environment, essentially reducing the variables in the experimental design. Besides yielding information about the barophilicity of certain amino acids, the experiment also provided valuable insight into the origin of the genetic code and its organizational influences. It was found that most of the amino acids that determined barophilicity were also found to be important in the organization of the genetic code. It was also found that more polar amino acids and smaller amino acids were more likely to be barophilic. Through the comparison of these two archaea, the conclusion was reached that the genetic code was likely structured under high hydrostatic pressure, and that hydrostatic pressure was a more influential factor in determining genetic code than temperature. == History ==