The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
A dynamic model for replication protein A (RPA) function in DNA processing pathways
Open accessAbstract
Processing of DNA in replication, repair and recombination pathways in cells of all organisms requires the participation of at least one major single-stranded DNA (ssDNA)-binding protein. This protein protects ssDNA from nucleolytic damage, prevents hairpin formation and blocks DNA reannealing until the processing pathway is successfully completed. Many ssDNA-binding proteins interact physically and functionally with a variety of other DNA processing proteins. These interactions are thought to temporally order and guide the parade of proteins that 'trade places' on the ssDNA, a model known as 'hand-off', as the processing pathway progresses. How this hand-off mechanism works remains poorly understood. Recent studies of the conserved eukaryotic ssDNA-binding protein replication protein A (RPA) suggest a novel mechanism by which proteins may trade places on ssDNA by binding to RPA and mediating conformation changes that alter the ssDNA-binding properties of RPA. This article reviews the structure and function of RPA, summarizes recent studies of RPA in DNA replication and other DNA processing pathways, and proposes a general model for the role of RPA in protein-mediated hand-off.
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Citations
Cites
Molecular Mechanisms of Mammalian DNA Repair and the DNA Damage Checkpoints
Sancar, A., Lindsey-Boltz, L. A., Ünsal-Kaçmaz, K., & Linn, S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073723 · Cited by 3,317
Sensing DNA Damage Through ATRIP Recognition of RPA-ssDNA Complexes
Zou, L., & Elledge, S. J. (2003) · Science · doi:10.1126/science.1083430 · Cited by 2,693
RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
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Replication Protein A phosphorylation and the cellular response to DNA damage
Binz, S. K., Sheehan, A. M., & Wold, M. S. (2004) · DNA Repair · doi:10.1016/j.dnarep.2004.03.028 · Cited by 299
Mechanisms of eukaryotic DNA double strand break repair
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“Rad9 RPA70, RPA32 NYD a (72) Rad17 RPA70, RPA32/14 NYD ae (70,71) p53BP1 RPA70, RPA32 NYD a (75) Nucleolin RPA14 645–707 ae (78,79) BRCA2 NYD N-terminus ae (76) XPG NYD NYD ae (22,118,119) XPF–ERCC1 NYD NYD ae (22,119,120)”
BackgroundDimerization of Human XPA and Formation of XPA2−RPA Protein Complex
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Cited by
ATR: an essential regulator of genome integrity
Cimprich, K. A., & Cortez, D. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2450 · Cited by 1,798
Regulation of Homologous Recombination in Eukaryotes
Heyer, W.-D., Ehmsen, K. T., & Liu, J. (2010) · Annual Review of Genetics · doi:10.1146/annurev-genet-051710-150955 · Cited by 1,066
ATR prohibits replication catastrophe by preventing global exhaustion of RPA
Toledo, L. I., Altmeyer, M., Rask, M.-B., Lukas, C., Larsen, D. H., Povlsen, L. K., Bekker-Jensen, S., Mailand, N., Bartek, J., & Lukas, J. (2013) · Cell · doi:10.1016/j.cell.2013.10.043 · Cited by 911
Maréchal, A., & Zou, L. (2015) · Cell Research · doi:10.1038/cr.2014.147 · Cited by 465
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
Metadata
- Authors
- Fanning, E.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-08-25
- Volume
- 34
- Issue
- 15
- Pages
- 4126-4137
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2135453449
- Cited by
- 571
- References
- 8
- FWCI
- 12.28
- Type
- journal article
- Language
- en
- Open access
- gold
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
