Cargando…

Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames

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 f...

Descripción completa

Detalles Bibliográficos
Autores principales: Daimon, Katsuya, Ishino, Sonoko, Imai, Namiko, Nagumo, Sachiyo, Yamagami, Takeshi, Matsukawa, Hiroaki, Ishino, Yoshizumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5911459/
https://www.ncbi.nlm.nih.gov/pubmed/29713633
http://dx.doi.org/10.3389/fmolb.2018.00037
_version_ 1783316211586564096
author Daimon, Katsuya
Ishino, Sonoko
Imai, Namiko
Nagumo, Sachiyo
Yamagami, Takeshi
Matsukawa, Hiroaki
Ishino, Yoshizumi
author_facet Daimon, Katsuya
Ishino, Sonoko
Imai, Namiko
Nagumo, Sachiyo
Yamagami, Takeshi
Matsukawa, Hiroaki
Ishino, Yoshizumi
author_sort Daimon, Katsuya
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5911459
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-59114592018-04-30 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 Front Mol Biosci Molecular Biosciences 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. Frontiers Media S.A. 2018-04-16 /pmc/articles/PMC5911459/ /pubmed/29713633 http://dx.doi.org/10.3389/fmolb.2018.00037 Text en Copyright © 2018 Daimon, Ishino, Imai, Nagumo, Yamagami, Matsukawa and Ishino. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Daimon, Katsuya
Ishino, Sonoko
Imai, Namiko
Nagumo, Sachiyo
Yamagami, Takeshi
Matsukawa, Hiroaki
Ishino, Yoshizumi
Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title_full Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title_fullStr Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title_full_unstemmed Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title_short Two Family B DNA Polymerases From Aeropyrum pernix, Based on Revised Translational Frames
title_sort two family b dna polymerases from aeropyrum pernix, based on revised translational frames
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5911459/
https://www.ncbi.nlm.nih.gov/pubmed/29713633
http://dx.doi.org/10.3389/fmolb.2018.00037
work_keys_str_mv AT daimonkatsuya twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT ishinosonoko twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT imainamiko twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT nagumosachiyo twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT yamagamitakeshi twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT matsukawahiroaki twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes
AT ishinoyoshizumi twofamilybdnapolymerasesfromaeropyrumpernixbasedonrevisedtranslationalframes