8C5Y

RPA tetrameric supercomplex from Pyrococcus abyssi

Summary for 8C5Y

• Entry DOI: 10.2210/pdb8c5y/pdb
• EMDB information: 15300 16444
• Descriptor: Replication factor A, RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination, RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination, ... (4 entities in total)
• Functional Keywords: dna replication, single strand dna-binding protein, rpa, dna binding protein
• Biological source: Pyrococcus abyssi; More
• Total number of polymer chains: 12
• Total formula weight: 217235.74

Authors

Madru, C.,Martinez-Carranza, M.,Legrand, P.,Sauguet, L. (deposition date: 2023-01-10, release date: 2023-05-03, Last modification date: 2024-07-24)

Primary citation

Madru, C.,Martinez-Carranza, M.,Laurent, S.,Alberti, A.C.,Chevreuil, M.,Raynal, B.,Haouz, A.,Le Meur, R.A.,Delarue, M.,Henneke, G.,Flament, D.,Krupovic, M.,Legrand, P.,Sauguet, L.
DNA-binding mechanism and evolution of replication protein A.
Nat Commun, 14:2326-2326, 2023

PubMed 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.

PubMed: 37087464
DOI: 10.1038/s41467-023-38048-w

Experimental method

ELECTRON MICROSCOPY (3.35 Å)