The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A single-molecule characterization of p53 search on DNA
Abstract
The tumor suppressor p53 slides along DNA while searching for its cognate site. Central to this process is the basic C-terminal domain, whose regulatory role and its coordination with the core DNA-binding domain is highly debated. Here we use single-molecule techniques to characterize the search process and disentangle the roles played by these two DNA-binding domains in the search process. We demonstrate that the C-terminal domain is capable of rapid translocation, while the core domain is unable to slide and instead hops along DNA. These findings are integrated into a model, in which the C-terminal domain mediates fast sliding of p53, while the core domain samples DNA by frequent dissociation and reassociation, allowing for rapid scanning of long DNA regions. The model further proposes how modifications of the C-terminal domain can activate “latent” p53 and reconciles seemingly contradictory data on the action of different domains and their coordination.
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In the citing paper
“The CTD is required for rapid linear diffusion of p53 on DNA,27 mediating fast sliding to facilitate the search for cognate p53 binding sites.28”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [28]
In the citing paper
“Through its interactions with DNA, the CTD mediates binding of p53 to non-specific DNA sites, enables rapid diffusion on DNA to facilitate the search for cognate target sites, and enhances the specificity for specific p53 recognition elements.15,27,28,65-67”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [28]
In the citing paper
“The CTD plays an essential role in facilitating the search for p53 target sites by promoting rapid one-dimensional sliding along the DNA helix and fast intersegmental transfer.28,67,70,71”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [28]
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Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607
Core domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
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Cited by
The multiple mechanisms that regulate p53 activity and cell fate
Hafner, A., Bulyk, M. L., Jambhekar, A., & Lahav, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0110-x · Cited by 1,129
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Direct observation of DNA target searching and cleavage by CRISPR-Cas12a
Jeon, Y., Choi, Y. H., Jang, Y., Yu, J., Goo, J., Lee, G., Jeong, Y. K., Lee, S. H., Kim, I.-S., Kim, J.-S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05245-x · Cited by 239
Terakawa, T., Higo, J., & Takada, S. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.026 · Cited by 32
Krois, A. S., Park, S., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00528 · Cited by 14
Metadata
- Authors
- Tafvizi, A., Huang, F., Fersht, A. R., Mirny, L. A., & van Oijen, A. M.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-12-22
- Volume
- 108
- Issue
- 2
- Pages
- 563-568
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 236
- References
- 2
- Language
- en
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- Tafvizi, A., Huang, F., Fersht, A. R., Mirny, L. A., & van Oijen, A. M. (2011). A single-molecule characterization of p53 search on DNA. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1016020107
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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.
