TY - JOUR
T1 - Comprehensive search for DNA polymerase in the hyperthermophilic archaeon, Pyrococcus furiosus
AU - Ishino, Sonoko
AU - Ishino, Yoshizumi
N1 - Funding Information:
Received 9 February 2006; accepted 16 February 2006. This work was supported by the Human Frontier Science Program (HFSP). This work was also supported in part by Grants-in Aid from the Ministry of Education, Science, and Sports to Y. I. We acknowledge the Hou-ansha foundation for the support of our work. This article is dedicated to Professor Eiko Ohtsuka on the occasion of her 70th birthday. Address correspondence to Yoshizumi Ishino, Department of Genetic Resources Technology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka-shi, Fukuoka 812-8581, Japan. E-mail: ishino@agr.kyushu-u.ac.jp
Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.
PY - 2006/6/1
Y1 - 2006/6/1
N2 - DNA polymerase activities were scanned in a Pyrococcus furiosus cell extract to identify all of the DNA polymerases in this organism. Three main fractions containing DNA polymerizing activity were subjected to Western blot analyses, which revealed that the main activities in each fraction were derived from three previously identified DNA polymerases. PCNA (proliferating cell nuclear antigen), the sliding clamp of DNA polymerases, did not bind tightly to any of the three DNA polymerases. A primer usage preference was also shown for each purified DNA polymerase. Considering their biochemical properties, the roles of the three DNA polymerases during DNA replication in the cells are discussed.
AB - DNA polymerase activities were scanned in a Pyrococcus furiosus cell extract to identify all of the DNA polymerases in this organism. Three main fractions containing DNA polymerizing activity were subjected to Western blot analyses, which revealed that the main activities in each fraction were derived from three previously identified DNA polymerases. PCNA (proliferating cell nuclear antigen), the sliding clamp of DNA polymerases, did not bind tightly to any of the three DNA polymerases. A primer usage preference was also shown for each purified DNA polymerase. Considering their biochemical properties, the roles of the three DNA polymerases during DNA replication in the cells are discussed.
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U2 - 10.1080/15257770600686485
DO - 10.1080/15257770600686485
M3 - Article
C2 - 16838855
AN - SCOPUS:33747617313
VL - 25
SP - 681
EP - 691
JO - Nucleosides, Nucleotides and Nucleic Acids
JF - Nucleosides, Nucleotides and Nucleic Acids
SN - 1525-7770
IS - 4-6
ER -