Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10122647/
https://www.ncbi.nlm.nih.gov/pubmed/37087464
http://dx.doi.org/10.1038/s41467-023-38048-w
_version_ 1785029537620295680
author 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
author_facet 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
author_sort Madru, Clément
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10122647
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-101226472023-04-24 DNA-binding mechanism and evolution of replication protein A 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 Nat Commun Article 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. Nature Publishing Group UK 2023-04-22 /pmc/articles/PMC10122647/ /pubmed/37087464 http://dx.doi.org/10.1038/s41467-023-38048-w Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
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
DNA-binding mechanism and evolution of replication protein A
title DNA-binding mechanism and evolution of replication protein A
title_full DNA-binding mechanism and evolution of replication protein A
title_fullStr DNA-binding mechanism and evolution of replication protein A
title_full_unstemmed DNA-binding mechanism and evolution of replication protein A
title_short DNA-binding mechanism and evolution of replication protein A
title_sort dna-binding mechanism and evolution of replication protein a
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10122647/
https://www.ncbi.nlm.nih.gov/pubmed/37087464
http://dx.doi.org/10.1038/s41467-023-38048-w
work_keys_str_mv AT madruclement dnabindingmechanismandevolutionofreplicationproteina
AT martinezcarranzamarkel dnabindingmechanismandevolutionofreplicationproteina
AT laurentsebastien dnabindingmechanismandevolutionofreplicationproteina
AT albertialessandrac dnabindingmechanismandevolutionofreplicationproteina
AT chevreuilmaelenn dnabindingmechanismandevolutionofreplicationproteina
AT raynalbertrand dnabindingmechanismandevolutionofreplicationproteina
AT haouzahmed dnabindingmechanismandevolutionofreplicationproteina
AT lemeurremya dnabindingmechanismandevolutionofreplicationproteina
AT delaruemarc dnabindingmechanismandevolutionofreplicationproteina
AT hennekeghislaine dnabindingmechanismandevolutionofreplicationproteina
AT flamentdidier dnabindingmechanismandevolutionofreplicationproteina
AT krupovicmart dnabindingmechanismandevolutionofreplicationproteina
AT legrandpierre dnabindingmechanismandevolutionofreplicationproteina
AT sauguetludovic dnabindingmechanismandevolutionofreplicationproteina