Abstract
Living organisms are divided into three domains, Bacteria, Eukarya, and Archaea. Comparative studies in the three domains have provided useful information to understand the evolution of the DNA replication machinery. DNA polymerase is the central enzyme of DNA replication. The presence of multiple family B DNA polymerases is unique in Crenarchaeota, as compared with other archaeal phyla, which have a single enzyme each for family B (PolB) and family D (PolD). We analyzed PolB1 and PolB3 in the hyperthermophilic crenarchaeon, Aeropyrum pernix, and found that they are larger proteins than those predicted from the coding regions in our previous study and from public database annotations. The recombinant larger PolBs exhibited the same DNA polymerase activities as previously reported. However, the larger PolB3 showed remarkably higher thermostability, which made this enzyme applicable to PCR. In addition, the high tolerance to salt and heparin suggests that PolB3 will be useful for amplification from the samples with contaminants, and therefore it has a great potential for diagnostic use in the medical and environmental field.
| Original language | English |
|---|---|
| Article number | 37 |
| Journal | Frontiers in Molecular Biosciences |
| Volume | 5 |
| Issue number | APR |
| DOIs | |
| Publication status | Published - Apr 16 2018 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
Cite this
Two family B DNA polymerases from Aeropyrum pernix, based on revised translational frames. / Daimon, Katsuya; Ishino, Sonoko; Imai, Namiko; Nagumo, Sachiyo; Yamagami, Takeshi; Matsukawa, Hiroaki; Ishino, Yoshizumi.
In: Frontiers in Molecular Biosciences, Vol. 5, No. APR, 37, 16.04.2018.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Two family B DNA polymerases from Aeropyrum pernix, based on revised translational frames
AU - Daimon, Katsuya
AU - Ishino, Sonoko
AU - Imai, Namiko
AU - Nagumo, Sachiyo
AU - Yamagami, Takeshi
AU - Matsukawa, Hiroaki
AU - Ishino, Yoshizumi
PY - 2018/4/16
Y1 - 2018/4/16
N2 - Living organisms are divided into three domains, Bacteria, Eukarya, and Archaea. Comparative studies in the three domains have provided useful information to understand the evolution of the DNA replication machinery. DNA polymerase is the central enzyme of DNA replication. The presence of multiple family B DNA polymerases is unique in Crenarchaeota, as compared with other archaeal phyla, which have a single enzyme each for family B (PolB) and family D (PolD). We analyzed PolB1 and PolB3 in the hyperthermophilic crenarchaeon, Aeropyrum pernix, and found that they are larger proteins than those predicted from the coding regions in our previous study and from public database annotations. The recombinant larger PolBs exhibited the same DNA polymerase activities as previously reported. However, the larger PolB3 showed remarkably higher thermostability, which made this enzyme applicable to PCR. In addition, the high tolerance to salt and heparin suggests that PolB3 will be useful for amplification from the samples with contaminants, and therefore it has a great potential for diagnostic use in the medical and environmental field.
AB - Living organisms are divided into three domains, Bacteria, Eukarya, and Archaea. Comparative studies in the three domains have provided useful information to understand the evolution of the DNA replication machinery. DNA polymerase is the central enzyme of DNA replication. The presence of multiple family B DNA polymerases is unique in Crenarchaeota, as compared with other archaeal phyla, which have a single enzyme each for family B (PolB) and family D (PolD). We analyzed PolB1 and PolB3 in the hyperthermophilic crenarchaeon, Aeropyrum pernix, and found that they are larger proteins than those predicted from the coding regions in our previous study and from public database annotations. The recombinant larger PolBs exhibited the same DNA polymerase activities as previously reported. However, the larger PolB3 showed remarkably higher thermostability, which made this enzyme applicable to PCR. In addition, the high tolerance to salt and heparin suggests that PolB3 will be useful for amplification from the samples with contaminants, and therefore it has a great potential for diagnostic use in the medical and environmental field.
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U2 - 10.3389/fmolb.2018.00037
DO - 10.3389/fmolb.2018.00037
M3 - Article
AN - SCOPUS:85045747044
VL - 5
JO - Frontiers in Molecular Biosciences
JF - Frontiers in Molecular Biosciences
SN - 2296-889X
IS - APR
M1 - 37
ER -