FN Archimer Export Format
PT J
TI Structural and functional determinants of the archaeal 8-oxoguanine-DNA glycosylase AGOG for DNA damage recognition and processing
BT 
AF Coste, Franck
   Goffinont, Stéphane
   Cros, Julien
   Gaudon, Virginie
   Guerin, Martine
   Garnier, Norbert
   Confalonieri, Fabrice
   FLAMENT, Didier
   Suskiewicz Marcin, Josef
   Castaing, Bertrand
AS 1:1;2:1;3:1;4:1;5:1;6:1;7:2;8:3;9:1;10:1;
FF 1:;2:;3:;4:;5:;6:;7:;8:PDG-REM-BEEP-LMEE;9:;10:;
C1 Centre de Biophysique Moléculaire (CBM), UPR4301 CNRS, Université d’Orléans , CS 80054, rue Charles Sadron , F-45071  Orléans cedex 02 , France
   Institut de Biologie Intégrative de la cellule (I2BC), UMR 9198 Université Paris-Saclay-CNRS-CEA , Bâtiment 21, Avenue de la Terrasse , F-91190  Gif-sur-Yvette , France
   Université de Brest, Ifremer, CNRS, Unité Biologie et Ecologie des Ecosystèmes marins Profonds (BEEP) , F-29280  Plouzané , France
C2 CNRS, FRANCE
   UNIV PARIS SACLAY, FRANCE
   IFREMER, FRANCE
SI BREST
SE PDG-REM-BEEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   DOAJ
   copubli-france
   copubli-univ-france
IF 14.9
TC 2
UR https://archimer.ifremer.fr/doc/00800/91216/96945.pdf
   https://archimer.ifremer.fr/doc/00800/91216/96946.pdf
LA English
DT Article
AB 8-Oxoguanine (GO) is a major purine oxidation product in DNA. Because of its highly mutagenic properties, GO absolutely must be eliminated from DNA. To do this, aerobic and anaerobic organisms from the three kingdoms of life have evolved repair mechanisms to prevent its deleterious effect on genetic integrity. The major way to remove GO is the base excision repair pathway, usually initiated by a GO-DNA glycosylase. First identified in bacteria (Fpg) and eukaryotes (OGG1), GO-DNA glycosylases were more recently identified in archaea (OGG2 and AGOG). AGOG is the less documented enzyme and its mode of damage recognition and removing remains to be clarified at the molecular and atomic levels. This study presents a complete structural characterisation of apo AGOGs from Pyrococcus abyssi (Pab) and Thermococcus gammatolerans (Tga) and the first structure of Pab-AGOG bound to lesion-containing single- or double-stranded DNA. By combining X-ray structure analysis, site directed mutagenesis and biochemistry experiments, we identified key amino acid residues of AGOGs responsible for the specific recognition of the lesion and the base opposite the lesion and for catalysis. Moreover, a unique binding mode of GO, involving double base flipping, never observed for any other DNA glycosylases, is revealed. In addition to unravelling the properties of AGOGs, our study, through comparative biochemical and structural analysis, offers new insights into the evolutionary plasticity of DNA glycosylases across all three kingdoms of life. 
PY 2022
PD OCT
SO Nucleic Acids Research
SN 0305-1048
PU Oxford University Press (OUP)
VL 50
IS 19
UT 000873924100001
BP 11072
EP 11092
DI 10.1093/nar/gkac932
ID 91216
ER

EF