title: Native PAGE to study the interaction between the oncosuppressor p53 and its protein ligands.
abstract: In the present study, we investigated a new approach for studying the interaction between p53 and MDM2/X (where MDM is murine double minute protein). The method is based on the different mobility between the interacting domains of the oncosuppressor p53 and its protein ligands MDM2/X on polyacrylamide gels under native conditions. While the two proteins MDM2/X alone were able to enter the gel, the formation of a binary complex between p53 and MDM2/X prevented the gel entry. The novel technique is reliable for determining the different affinity elicited by MDM2 or MDMX toward p53, and can be useful for analyzing the dissociation power exerted by other molecules on the p53-MDM2/X complex.
authors.affiliation: Department of Movement Sciences and Wellness, University of Naples "Parthenope,", Naples, Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: Lamberti
authors.forename: Roberta
authors.initials: R
authors.lastname: Sgammato
authors.forename: Doriana
authors.initials: D
authors.lastname: Desiderio
authors.forename: Chiara
authors.initials: C
authors.lastname: Punzo
authors.forename: Gennaro
authors.initials: G
authors.lastname: Raimo
authors.forename: Ettore
authors.initials: E
authors.lastname: Novellino
authors.forename: Alfonso
authors.initials: A
authors.lastname: Carotenuto
authors.forename: Mariorosario
authors.initials: M
authors.lastname: Masullo
mesh_terms: D008024:Ligands; D063347:Native Polyacrylamide Gel Electrophoresis / Q000379:methods*; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping / Q000379:methods; D051736:Proto-Oncogene Proteins c-mdm2 / Q000032:analysis / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000032:analysis / Q000378:metabolism*
chemical_list: D008024:Ligands; D016159:Tumor Suppressor Protein p53; D051736:Proto-Oncogene Proteins c-mdm2
keywords: Complex formation; MDM2; MDMX; Native PAGE; p53