FN Archimer Export Format
PT J
TI The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: A multifunctional enzyme for initiation and repair?
BT 
AF LE BRETON, Magali
   HENNEKE, Ghislaine
   NORAIS, C
   FLAMENT, Didier
   MYLLYKALLIO, H
   QUERELLOU, Joel
   RAFFIN, Jean-Paul
AS 1:1;2:1;3:2;4:1;5:2;6:1;7:1;
FF 1:;2:PDG-DOP-DCB-EEP-LMEE;3:;4:PDG-DOP-DCB-EEP-LMEE;5:;6:PDG-DOP-DCB-EEP-LMEE;7:;
C1 Ifremer, UMR6197, Lab Microbiol Enviornm Extremes, F-29280 Plouzane, France.
   Univ Paris 11, Inst Genet & Microbiol, UMR8621, F-91405 Orsay, France.
C2 IFREMER, FRANCE
   UNIV PARIS 11, FRANCE
SI BREST
SE PDG-DOP-DCB-EEP-LMEE
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 4.472
TC 36
UR https://archimer.ifremer.fr/doc/2007/publication-3520.pdf
LA English
DT Article
DE ;Strand displacement;Gap filling;DNA primase;Archaea;DNA replication
AB We report on the characterization of the DNA primase complex of the hyperthermophilic archaeon Pyrococcus abyssi (Pab). The Pab DNA primase complex is composed of the proteins Pabp41 and Pabp46, which show sequence similarities to the p49 and p58 subunits, respectively, of the eukaryotic polymerase alpha-primase complex. Both subunits were expressed, purified, and characterized. The Pabp41 subunit alone had no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increased the rate of DNA synthesis but decreased the length of the DNA fragments synthesized and conferred RNA synthesis capability. Moreover, in our experimental conditions, Pab DNA primase had comparable affinities for ribonucleotides and deoxyribonu-cleotides, and its activity was dependent on the presence of Mg2+ and Mn2+. Interestingly, Pab DNA primase also displayed DNA polymerase, gap-filling, and strand-displacement activities. Genetic analyses undertaken in Haloferax volcanii suggested that the eukaryotic-type heterodimeric primase is essential for survival in archaeal cells. Our results are in favor of a multifunctional archaeal primase involved in priming and repair. (c) 2007 Elsevier Ltd. All rights reserved.
PY 2007
PD DEC
SO Journal of Molecular Biology
SN 0022-2836
PU Elsevier
VL 374
IS 5
UT 000251701100004
BP 1172
EP 1185
DI 10.1016/j.jmb.2007.10.015
ID 3520
ER

EF