DNA-binding mechanism and evolution of Replication Protein A
Open accessPreprint — published as 10.1038/s41467-023-38048-w
Abstract
Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair, in both eukaryotic and archaeal cells. By using an integrative approach that combines three crystal structures, four cryo-EM structures in complex with single-stranded DNA (ssDNA) of different lengths, we extensively characterized RPA from Pyrococcus abyssi in different states. These structures show two essential features conserved in eukaryotes: a trimeric core and a module that promotes cooperative binding to ssDNA, as well as a newly identified archaeal-specific domain. These structures reveal for the first time how ssDNA is handed over from one RPA complex to the other, and uncover an unanticipated mechanism of self-association on ssDNA tracts. This work constitutes a significant step forward in the molecular understanding of the structure and DNA-binding mechanism of RPA, with far-reaching implications for the evolution of this primordial replication factor in Archaea and Eukarya.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
The structure of human CST reveals a decameric assembly bound to telomeric DNA
Lim, C. J., Barbour, A. T., Zaug, A. J., Goodrich, K. J., McKay, A. E., Wuttke, D. S., & Cech, T. R. (2020) · Science · doi:10.1126/science.aaz9649 · Cited by 111 · see citing works
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- Authors
- Madru, C., Martinez-Carranza, M., Laurent, S., Alberti, A. C., Chevreuil, M., Raynal, B., Haouz, A., Le Meur, R. A., Delarue, M., Flament, D., Krupovic, M., Legrand, P., & Sauguet, L.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Sauguet, Ludovic
- ORCID
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2022-07-21
- Volume
- 14
- Issue
- 1
- Pages
- 2326-2326
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10122647
- OpenAlex
- W4366769395
- Cited by
- 23
- References
- 2
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 10 · 2023: 1
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- Institutional Archive of Ifremer (French Research Institute for Exploitation of the Sea) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANR-20-CE11-0003, ANR-17-CE11-0005)
- Fondation pour la Recherche Médicale
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- replication protein A, single-stranded DNA binding, Pyrococcus abyssi, OB-fold, DNA replication, DNA repair, DNA recombination, replisome, protein-DNA interactions
- MeSH terms
- DNA, DNA Repair, DNA Replication, DNA, Single-Stranded, Protein Binding, Replication Protein A
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