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Article

Tight DNA binding and oligomerization are dispensable for the ability of p53 to transactivate target genes and suppress transformation.

The EMBO journal - 1 Jul 1993

Shaulian E, Zauberman A, Milner J, Davies E A, Oren M

Abstract excerpt

The p53 tumor suppressor protein can bind tightly to specific sequence elements in the DNA and induce the transactivation of genes harboring such p53 binding sites. Various lines of evidence suggest that p53 binds to its target site as an oligomer. To test whether oligomerization is essential for the biological and biochemical activities of p53, we deleted a major part of the dimerization domain of mouse...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 8334995
DOI: 10.1002/j.1460-2075.1993.tb05940.x
PMCID: PMC413529

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Tight DNA binding and oligomerization are dispensable for the ability of p53 to transactivate target genes and suppress transformation.PMID 8334995Read ↗

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Functional domains of wild-type and mutant p53 proteins involved in transcriptional regulation, transdominant inhibition, and transformation suppression.Semantic proximity Read ↗

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The Status of p53 Oligomeric and Aggregation States in CancerSemantic proximity Read ↗

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Conservation of DNA-binding specificity and oligomerisation properties within the p53 familySemantic proximity Read ↗

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The Ashkenazi-Centric G334R Variant of TP53 is Severely Impaired for Transactivation but Retains Tumor Suppressor Function in a Mouse Model.Semantic proximity Read ↗

The role of tetramerization in p53 function.Semantic proximity Read ↗

Dimerization: a versatile switch for oncogenesisSemantic proximity Read ↗

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