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P53 is a homotetrameric transcription factor known to interact with the ankyrin protein 53BP2 (a fragment of the ASPP2 protein). NF-\u03baB is also regulated by ankyrin proteins, the prototype of which is the I\u03baB family. The DNA binding sequences of the two transcription factors are similar, sharing 8 out of 10 nucleotides. Interactions between the two proteins, both direct and indirect, have been noted previously and the two proteins play central roles in the control of proliferation and apoptosis.<\/jats:p>\n                     <\/jats:sec><jats:sec>\n                        <jats:title>Results<\/jats:title>\n                        <jats:p>Using previously published structure data, we noted a significant degree of structural alignment between p53 and NF-\u03baB p65. We also determined that I\u03baB\u03b1 and p53 bind <jats:italic>in vitro<\/jats:italic> through a specific interaction in part involving the DNA binding region of p53, or a region proximal to it, and the amino terminus of I\u03baB\u03b1 independently or cooperatively with the ankyrin 3 domain of I\u03baB\u03b1 In cotransfection experiments, \u03baB\u03b1 could significantly inhibit the transcriptional activity of p53. Inhibition of p53-mediated transcription was increased by deletion of the ankyrin 2, 4, or 5 domains of I\u03baB\u03b1 Co-precipitation experiments using the stably transfected ankyrin 5 deletion mutant of \u03baB\u03b1 and endogenous wild-type p53 further support the hypothesis that p53 and I\u03baB\u03b1 can physically interact <jats:italic>in vivo<\/jats:italic>.<\/jats:p>\n                     <\/jats:sec><jats:sec>\n                        <jats:title>Conclusion<\/jats:title>\n                        <jats:p>The aggregate results obtained using bacterially produced I\u03baB\u03b1 and p53 as well as reticulocyte lysate produced proteins suggest a correlation between <jats:italic>in vitro<\/jats:italic> co-precipitation in at least one of the systems and <jats:italic>in vivo<\/jats:italic> p53 inhibitory activity. These observations argue for a mechanism involving direct binding of I\u03baB\u03b1 to p53 in the inhibition of p53 transcriptional activity, analogous to the inhibition of NF-\u03baB by \u03baB\u03b1 and p53 by 53BP2\/ASPP2. These data furthermore suggest a role for ankyrin proteins in the regulation of p53 activity. Taken together, the NF\u03baB and p53 proteins share similarities in structure, DNA binding sites and binding and regulation by ankyrin proteins in support of our hypothesis that the two proteins share common descent from an ancestral transcriptional factor.<\/jats:p>\n                     <\/jats:sec>","DOI":"10.1186\/1471-2172-6-12","type":"journal-article","created":{"date-parts":[[2005,6,21]],"date-time":"2005-06-21T18:13:54Z","timestamp":1119377634000},"update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Modulation of p53 activity by I\u03baB\u03b1: Evidence suggesting a common phylogeny between NF-\u03baB and p53 transcription factors"],"prefix":"10.1186","volume":"6","author":[{"given":"David H","family":"Dreyfus","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masayuki","family":"Nagasawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erwin W","family":"Gelfand","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lucy Y","family":"Ghoda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2005,6,21]]},"reference":[{"key":"73_CR1","doi-asserted-by":"publisher","first-page":"1054","DOI":"10.1101\/gad.10.9.1054","volume":"10","author":"LJ Ko","year":"1996","unstructured":"Ko LJ, Prives C: p53: puzzle and paradigm. 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