DNA-binding mechanism and evolution of replication protein A

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 appr...

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Bibliographic Details
Published in:	Nature communications Vol. 14; no. 1; p. 2326
Main Authors:	Madru, Clément, Martínez-Carranza, Markel, Laurent, Sébastien, 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
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 22-04-2023 Nature Publishing Group Nature Portfolio
Subjects:	101/28 631/337/151/2353 631/535/1258/1259 82/103 9/10 Archaea Clustering Deoxyribonucleic acid DNA DNA - metabolism DNA biosynthesis DNA Repair DNA Replication DNA, Single-Stranded DNA, Single-Stranded - genetics DNA-binding protein Domains Eukaryotes Evolution Humanities and Social Sciences Life Sciences multidisciplinary Protein A Protein Binding Protein structure Proteins Recombination Replication Replication Protein A Replication Protein A - metabolism Science Science (multidisciplinary)
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Summary:	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. Here the authors present the structure of Replication Protein A (RPA) in Archaea. The RPA structure from P. abyssi has been determined in presence and absence of DNA, providing insights into the evolution of this replication factor in eukaryotes
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 PMCID: PMC10122647
ISSN:	2041-1723 2041-1723
DOI:	10.1038/s41467-023-38048-w