FN Archimer Export Format
PT J
TI DNA polymerase switching on homotrimeric PCNA at the replication fork of the euryarchaea Pyrococcus abyssi
BT 
AF ROUILLON, Christophe
   HENNEKE, Ghislaine
   FLAMENT, Didier
   QUERELLOU, Joel
   RAFFIN, Jean-Paul
AS 1:1;2:1;3:1;4:1;5:1;
FF 1:PDG-DOP-DCB-EEP-LMEE;2:PDG-DOP-DCB-EEP-LMEE;3:PDG-DOP-DCB-EEP-LMEE;4:PDG-DOP-DCB-EEP-LMEE;5:;
C1 IFREMER, UMR 6197, Lab Microbiol & Environm Extremes, F-29280 Plouzane, France.
C2 IFREMER, FRANCE
SI BREST
SE PDG-DOP-DCB-EEP-LMEE
IN WOS Ifremer jusqu'en 2018
IF 4.472
TC 28
UR https://archimer.ifremer.fr/doc/2007/publication-2638.pdf
LA English
DT Article
DE ;RF C;PCNA loading;DNA polymerase switching;DNA replication;Archaea
AB DNA replication in Archaea, as in other organisms, involves large protein complexes called replisomes. In the Euryarchaeota subdomain, only two putative replicases have been identified, and their roles in leading and lagging strand DNA synthesis are still poorly understood. In this study, we focused on the coupling of proliferating cell nuclear antigen (PCNA)loading mechanisms with DNA polymerase function in the Euryarchaea Pyrococcus abyssi. PCNA spontaneously loaded onto primed DNA, and replication factor C dramatically increased this loading. Surprisingly, the family B DNA polymerase (Pol B) also increased PCNA loading, probably by stabilizing the clamp on primed DNA via an essential motif. In contrast, on an RNA-primed DNA template, the PCNA/Pol B complex was destabilized in the presence of dNTPs, allowing the family D DNA polymerase (Pol D) to perform RNA-primed DNA synthesis. Then, Pol D is displaced by Pol B to perform processive DNA synthesis, at least on the leading strand. (C) 2007 Elsevier Ltd. All rights reserved.
PY 2007
PD JUL
SO Journal of Molecular Biology
SN 0022-2836
PU Elsevier
VL 369
IS 2
UT 000246757600005
BP 343
EP 355
DI 10.1016/j.jmb.2007.03.054
ID 2638
ER

EF