DNA-binding mechanism and evolution of replication protein A

Clément Madru, Markel Martínez-Carranza, Sébastien Laurent, Alessandra C. Alberti, Maelenn Chevreuil, Bertrand Raynal, Ahmed Haouz, Rémy A. Meur, Marc Delarue, Ghislaine Henneke, Didier Flament, Mart Krupovic, Pierre Legrand and Ludovic Sauguet ()
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Clément Madru: Institut Pasteur, Université Paris Cité, CNRS
Markel Martínez-Carranza: Institut Pasteur, Université Paris Cité, CNRS
Sébastien Laurent: Univ Brest, Ifremer, CNRS, Biologie et Ecologie des Ecoystèmes marins profonds (BEEP)
Alessandra C. Alberti: Institut Pasteur, Université Paris Cité, CNRS
Maelenn Chevreuil: C2RT, Institut Pasteur, Université Paris Cité, CNRS
Bertrand Raynal: C2RT, Institut Pasteur, Université Paris Cité, CNRS
Ahmed Haouz: C2RT, Institut Pasteur, Université Paris Cité, CNRS
Rémy A. Meur: C2RT, Institut Pasteur, Université Paris Cité, CNRS
Marc Delarue: Institut Pasteur, Université Paris Cité, CNRS
Ghislaine Henneke: Univ Brest, Ifremer, CNRS, Biologie et Ecologie des Ecoystèmes marins profonds (BEEP)
Didier Flament: Univ Brest, Ifremer, CNRS, Biologie et Ecologie des Ecoystèmes marins profonds (BEEP)
Mart Krupovic: Institut Pasteur, Université Paris Cité, CNRS
Pierre Legrand: Institut Pasteur, Université Paris Cité, CNRS
Ludovic Sauguet: Institut Pasteur, Université Paris Cité, CNRS

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-38048-w

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