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Article Dans Une Revue Nature Communications Année : 2023

DNA-binding mechanism and evolution of replication protein A

Mart Krupovic

Résumé

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 ( A cidic R pa1 O B-binding D omain), 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.
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Origine : Publication financée par une institution
licence : CC BY - Paternité

Dates et versions

hal-04112308 , version 1 (01-06-2023)

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Paternité

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Clément Madru, Markel Martínez-Carranza, Sébastien Laurent, Alessandra Alberti, Maelenn Chevreuil, et al.. DNA-binding mechanism and evolution of replication protein A. Nature Communications, 2023, 14 (1), pp.2326. ⟨10.1038/s41467-023-38048-w⟩. ⟨hal-04112308⟩
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