The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA
Abstract
The multidomain homotetrameric tumor suppressor p53 has two modes of binding dsDNA that are thought to be responsible for scanning and recognizing specific response elements (REs). The C termini bind nonspecifically to dsDNA. The four DNA-binding domains (DBDs) bind REs that have two symmetric 10 base-pair sequences. p53 bound to a 20-bp RE has the DBDs enveloping the DNA, which is in the center of the molecule surrounded by linker sequences to the tetramerization domain (Tet). We investigated by electron microscopy structures of p53 bound to DNA sequences consisting of a 20-bp RE with either 12 or 20 bp nonspecific extensions on either end. We found a variety of structures that give clues to recognition and scanning mechanisms. The 44- and 60-bp sequences gave rise to three and four classes of structures, respectively. One was similar to the known 20-bp structure, but the DBDs in the other classes were loosely arranged and incompatible with specific DNA recognition. Some of the complexes had density consistent with the C termini extending from Tet to the DNA, adjacent to the DBDs. Single-molecule fluorescence resonance energy transfer experiments detected the approach of the C termini towards the DBDs on addition of DNA. The structural data are consistent with p53 sliding along DNA via its C termini and the DNA-binding domains hopping on and off during searches for REs. The loose structures and posttranslational modifications account for the affinity of nonspecific DNA for p53 and point to a mechanism of enhancement of specificity by its binding to effector proteins.
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In the citing paper
“Our data are consistent with electron microscopy and single molecule FRET studies which show that the p53 tetramer can adopt a closed conformation on DNA in which the CTD and DBD approach more closely than in the unbound state.66”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [66]
In the citing paper
“While the TET domain is expected to be positioned on the opposite side of the DNA relative to the four DBDs,65,66,68”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [66]
In the citing paper
“In the absence of DNA, p53 forms an open cross-shaped structure with loosely coupled dimers interacting via the core domain.”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Melero et al. 2011
In the citing paper
“On DNA binding, the structure of p53 rigidifies, becoming more compacted.”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Melero et al. 2011
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Citations
Cites
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551 · cited 1×
“These structures show varying dimer-dimer contacts and the overall assembly of the core domains on DNA is radically different from the one described in the first DBD · DNA complex solved (23).”
BackgroundDefinition of a consensus binding site for p53
El-Deiry, W. S., Kern, S. E., Pietenpol, J. A., Kinzler, K. W., & Vogelstein, B. (1992) · Nature Genetics · doi:10.1038/ng0492-45 · Cited by 1,985
How p53 binds DNA as a tetramer
McLure, K. G., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3342 · Cited by 260
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Cited by
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
Self-citationStructural Evolution and Dynamics of the p53 Proteins
Chillemi, G., Kehrloesser, S., Bernassola, F., Desideri, A., Dötsch, V., Levine, A. J., & Melino, G. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a028308 · Cited by 65
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
- Melero, R., Rajagopalan, S., Lázaro, M., Joerger, A. C., Brandt, T., Veprintsev, D. B., Lasso, G., Gil, D., Scheres, S. H. W., Carazo, J. M., Fersht, A. R., & Valle, M.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-12-22
- Volume
- 108
- Issue
- 2
- Pages
- 557-562
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 64
- References
- 4
- Language
- en
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- Melero, R., Rajagopalan, S., Lázaro, M., Joerger, A. C., Brandt, T., Veprintsev, D. B., Lasso, G., Gil, D., Scheres, S. H. W., Carazo, J. M., Fersht, A. R., & Valle, M. (2011). Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1015520107
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