ArticleNucleic acids research2011
Sequence-dependent cooperative binding of p53 to DNA targets and its relationship to the structural properties of the DNA targets.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed.
- Nucleosome binding by TP53, TP63, and TP73 is determined by the composition, accessibility, and helical orientation of their binding sites.Genome research · 2025Article
- A molecular mechanism for the "digital" response of p53 to stress.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Optimisation of TP53 reporters by systematic dissection of synthetic TP53 response elements.Nucleic acids research · 2023Article
- Sequence Properties of An Intramolecular Interaction That Inhibits p53 DNA Binding.Biomolecules · 2022Article
- Evolutionary history of the p53 family DNA-binding domain: insights from an Alvinella pompejana homolog.Cell death & disease · 2022Article
- Article
- Adaptive homeostasis and the p53 isoform network.EMBO reports · 2021Review
- Rely on Each Other: DNA Binding Cooperativity Shapes p53 Functions in Tumor Suppression and Cancer Therapy.Cancers · 2021Review
- The complex architecture of p53 binding sites.Nucleic acids research · 2021Article
- Article
- Article
- Global Regulatory Roles of the Histidine-Responsive Transcriptional Repressor HutC in Pseudomonas fluorescens SBW25.Journal of bacteriology · 2020Article
- The multiple mechanisms that regulate p53 activity and cell fate.Nature reviews. Molecular cell biology · 2019Review
- Structural basis of gene regulation by the Grainyhead/CP2 transcription factor family.Nucleic acids research · 2018Article
- Post-translational regulation of p53 function through 20S proteasome-mediated cleavage.Cell death and differentiation · 2017Article
- Diverse p53/DNA binding modes expand the repertoire of p53 response elements.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The p53 C terminus controls site-specific DNA binding and promotes structural changes within the central DNA binding domain.Molecular cell · 2015Article
- Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics.Chemical reviews · 2015Review
- miR-23b as a potential tumor suppressor and its regulation by DNA methylation in cervical cancer.Infectious agents and cancer · 2015Article
- Spec-seq: determining protein-DNA-binding specificity by sequencing.Briefings in functional genomics · 2015Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prime mechanism by which p53 acts as a tumor suppressor is as a transcription factor regulating the expression of diverse downstream genes. The DNA-binding domain of p53 (p53DBD) interacts with defined DNA sites and is the main target for mutations in human primary tumors. Here, we show that the CWWG motif, found in the center of each consensus p53 half-site, is a key player in p53/DNA interactions. Gel-mobility-shift assays provide a unique opportunity to directly observe the various oligomeric complexes formed between p53DBD and its target sites. We demonstrate that p53DBD binds to p53 consensus sites containing CATG with relatively low cooperativity, as both dimers and tetramers, and with even lower cooperativity to such sites containing spacer sequences. p53DBD binds to sites containing CAAG and CTAG with measurable affinity only when imbedded in two contiguous p53 half-sites and only as tetramers (with very high cooperativity). There are three orders-of-magnitude difference in the cooperativity of interaction between sites differing in their non-contacted step, and further two orders-of-magnitude difference as a function of spacer sequences. By experimentally measuring the global structural properties of these sites, by cyclization kinetics of DNA minicircles, we correlate these differences with the torsional flexibility of the binding sites.
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