FN Archimer Export Format
PT J
TI The hyperthermophilic euryarchaeota Pyrococcus abyssi likely requires the two DNA polymerases D and B for DNA replication
BT 
AF HENNEKE, Ghislaine
   FLAMENT, Didier
   HUBSCHER, Ulrich
   QUERELLOU, Joel
   RAFFIN, Jean-Paul
AS 1:1;2:1;3:2;4:1;5:1;
FF 1:PDG-DOP-DCB-EEP-LMEE;2:PDG-DOP-DCB-EEP-LMEE;3:;4:PDG-DOP-DCB-EEP-LMEE;5:;
C1 IFREMER, UMR 6197, Lab Microbiol & Environm Extremes, DRV,VP,LM2E, F-29280 Plouzane, France.
   Univ Zurich, Inst Vet Biochem, CH-8057 Zurich, Switzerland.
C2 IFREMER, FRANCE
   UNIV ZURICH, SWITZERLAND
SI BREST
SE PDG-DOP-DCB-EEP-LMEE
IN WOS Ifremer jusqu'en 2018
   copubli-int-hors-europe
IF 5.229
TC 76
UR https://archimer.ifremer.fr/doc/2005/publication-423.pdf
LA English
DT Article
DE ;DNA polymerase;Strand displacement;Gap filling;Euryarchaea;DNA replication
AB DNA polymerases carry out DNA synthesis during DNA replication, DNA recombination and DNA repair. During the past five years, the number of DNA polymerases in both eukarya and bacteria has increased to at least 19 and multiple biological roles have been assigned to many DNA polymerases. Archaea, the third domain of life, on the other hand, have only a subset of the eukaryotic-like DNA polymerases. The diversity among the archaeal DNA polymerases poses the intriguing question of their functional tasks. Here, we focus on the two identified DNA polymerases, the family B DNA polymerase B (PabpolB) and the family D DNA polymerase D (PabpolD) from the hyperthermophilic euryarchaeota Pyrococcus abyssi. Our data can be summarized as follows: (i) both Pabpols are DNA polymerizing enzymes exclusively; (ii) their DNA binding properties as tested in gel shift competition assays indicated that PabpolD has a preference for a primed template; (iii) PabPolD is a primer-directed DNA polymerase independently of the primer composition whereas PabpolB behaves as an exclusively DNA primer-directed DNA polymerase; (iv) PabPCNA is required for PabpolD to perform efficient DNA synthesis but not PabpolB; (v) PabpolD, but not PabpolB, contains strand displacement activity; (vii) in the presence of PabPCNA, however, both Pabpols D and B show strand displacement activity; and (viii) we show that the direct interaction between PabpolD and PabPCNA is DNA-dependent. Our data imply that PabPolD might play an important role in DNA replication likely together with PabpolB, suggesting that archaea require two DNA polymerases at the replication fork. 
PY 2005
PD JUN
SO Journal of Molecular Biology
SN 0022-2836
PU Elsevier
VL 350
IS 1
UT 000230021200006
BP 53
EP 64
DI 10.1016/j.jmb.2005.04.042
ID 423
ER

EF