FN Archimer Export Format
PT J
TI The interplay at the replisome mitigates the impact of oxidative damage on the genetic integrity of hyperthermophilic Archaea
BT 
AF Killelea, Tom
   Palud, Adeline
   Akcha, Farida
   Lemor, Mélanie
   L'haridon, Stephane
   Godfroy, Anne
   Henneke, Ghislaine
AS 1:3;2:1;3:2;4:3;5:3;6:1;7:1;
FF 1:;2:PDG-REM-EEP-LMEE;3:PDG-RBE-BE-LEX;4:;5:;6:PDG-REM-EEP-LMEE;7:PDG-REM-EEP-LMEE;
C1 Univ Brest, Ifremer, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, Plouzané, France
   Laboratoire d'Ecotoxicologie, Ifremer, Nantes, France
   Univ Brest, Ifremer, CNRS, Laboratoire de Microbiologie des Environnements Extrêmes, Plouzané, France
C2 IFREMER, FRANCE
   IFREMER, FRANCE
   UBO, FRANCE
SI BREST
   NANTES
SE PDG-REM-EEP-LMEE
   PDG-RBE-BE-LEX
UM BEEP-LM2E
IN WOS Ifremer UPR
   WOS Ifremer UMR
   WOS Cotutelle UMR
   DOAJ
   copubli-france
   copubli-univ-france
IF 7.08
TC 8
UR https://archimer.ifremer.fr/doc/00502/61372/64989.pdf
LA English
DT Article
AB 8-oxodeoxyguanosine (8-oxodG), a major oxidised base modification, has been investigated to study its impact on DNA replication in hyperthermophilic Archaea. Here we show that 8-oxodG is formed in the genome of growing cells, with elevated levels following exposure to oxidative stress. Functional characterisation of cell-free extracts and the DNA polymerisation enzymes, PolB, PolD, and the p41/p46 complex, alone or in the presence of accessory factors (PCNA and RPA) indicates that translesion synthesis occurs under replicative conditions. One of the major polymerisation effects was stalling, but each of the individual proteins could insert and extend past 8-oxodG with differing efficiencies. The introduction of RPA and PCNA influenced PolB and PolD in similar ways, yet provided a cumulative enhancement to the polymerisation performance of p41/p46. Overall, 8-oxodG translesion synthesis was seen to be potentially mutagenic leading to errors that are reminiscent of dA:8-oxodG base pairing. 
PY 2019
PD JUL
SO Elife
SN 2050-084X
PU eLife Sciences Publications, Ltd
VL 8
UT 000471216300001
DI 10.7554/eLife.45320
ID 61372
ER

EF