FN Archimer Export Format
PT J
TI DNA-binding mechanism and evolution of replication protein A
BT 
AF Madru, Clément
   Martínez-Carranza, Markel
   Laurent, Sebastien
   Alberti, Alessandra C.
   Chevreuil, Maelenn
   Raynal, Bertrand
   Haouz, Ahmed
   Le Meur, Rémy A.
   Delarue, Marc
   Henneke, Ghislaine
   Flament, Didier
   Krupovic, Mart
   Legrand, Pierre
   Sauguet, Ludovic
AS 1:1;2:1;3:2;4:1;5:3;6:3;7:4;8:5;9:1;10:2;11:2;12:6;13:1,7;14:1;
FF 1:;2:;3:PDG-REM-BEEP-LMEE;4:;5:;6:;7:;8:;9:;10:PDG-REM-BEEP-LMEE;11:PDG-REM-BEEP-LMEE;12:;13:;14:;
C1 Architecture and Dynamics of Biological Macromolecules, Institut Pasteur, Université Paris Cité, CNRS, UMR 3528, Paris, France
   Univ Brest, Ifremer, CNRS, Biologie et Ecologie des Ecoystèmes marins profonds (BEEP), F-29280, Plouzané, France
   Molecular Biophysics Platform, C2RT, Institut Pasteur, Université Paris Cité, CNRS, UMR 3528, Paris, France
   Crystallography Platform, C2RT, Institut Pasteur, Université Paris Cité, CNRS, UMR 3528, Paris, France
   Biological NMR Platform & HDX, C2RT, Institut Pasteur, Université Paris Cité, CNRS, UMR 3528, Paris, France
   Archaeal Virology Unit, Institut Pasteur, Université Paris Cité, CNRS, UMR 6047, Paris, France
   Synchrotron SOLEIL, HelioBio group, L’Orme des Merisiers, 91190, Saint-Aubin, France
C2 INST PASTEUR, FRANCE
   IFREMER, FRANCE
   INST PASTEUR, FRANCE
   INST PASTEUR, FRANCE
   INST PASTEUR, FRANCE
   INST PASTEUR, FRANCE
   SYNCHROTRON SOLEIL, FRANCE
SI BREST
SE PDG-REM-BEEP-LMEE
UM BEEP-LM2E
IN WOS Ifremer UMR
   DOAJ
   copubli-france
IF 16.6
TC 4
UR https://archimer.ifremer.fr/doc/00834/94613/101996.pdf
   https://archimer.ifremer.fr/doc/00834/94613/101997.pdf
   https://archimer.ifremer.fr/doc/00834/94613/101998.pdf
   https://archimer.ifremer.fr/doc/00834/94613/101999.pdf
   https://archimer.ifremer.fr/doc/00834/94613/102000.mp4
   https://archimer.ifremer.fr/doc/00834/94613/102001.mp4
   https://archimer.ifremer.fr/doc/00834/94613/102002.pdf
   https://archimer.ifremer.fr/doc/00834/94613/102003.xlsx
LA English
DT Article
AB Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little is known about the structure of RPA in Archaea, the third domain of life. By using an integrative structural, biochemical and biophysical approach, we extensively characterize RPA from Pyrococcus abyssi in the presence and absence of DNA. The obtained X-ray and cryo-EM structures reveal that the trimerization core and interactions promoting RPA clustering on ssDNA are shared between archaea and eukaryotes. However, we also identified a helical domain named AROD (Acidic Rpa1 OB-binding Domain), and showed that, in Archaea, RPA forms an unanticipated tetrameric supercomplex in the absence of DNA. The four RPA molecules clustered within the tetramer could efficiently coat and protect stretches of ssDNA created by the advancing replisome. Finally, our results provide insights into the evolution of this primordial replication factor in eukaryotes. 
PY 2023
PD APR
SO Nature Communications
SN 2041-1723
PU Springer Science and Business Media LLC
VL 14
IS 1
UT 000984264200007
DI 10.1038/s41467-023-38048-w
ID 94613
ER

EF