ŠEBEST, Peter, Marie BRÁZDOVÁ, Miroslav FOJTA and Hana PIVOŇKOVÁ. Differential Salt-Induced Dissociation of the p53 Protein Complexes with Circular and Linear Plasmid DNA Substrates Suggest Involvement of a Sliding Mechanism. International Journal of Molecular Sciences. Basel: MDPI Center, 2015, vol. 16, No 2, p. 3163-3177. ISSN 1422-0067. doi:10.3390/ijms16023163.
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Basic information
Original name Differential Salt-Induced Dissociation of the p53 Protein Complexes with Circular and Linear Plasmid DNA Substrates Suggest Involvement of a Sliding Mechanism
Authors ŠEBEST, Peter (203 Czech Republic), Marie BRÁZDOVÁ (203 Czech Republic), Miroslav FOJTA (203 Czech Republic, guarantor, belonging to the institution) and Hana PIVOŇKOVÁ (203 Czech Republic).
Edition International Journal of Molecular Sciences, Basel, MDPI Center, 2015, 1422-0067.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 3.257
RIV identification code RIV/00216224:14740/15:00081384
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.3390/ijms16023163
UT WoS 000350333600051
Keywords in English TUMOR-SUPPRESSOR P53; CISPLATIN-DAMAGED DNA; SUPERCOILED DNA; MERCURY-ELECTRODE; BINDING; CONFORMATION; SPECIFICITY; KINETICS; DOMAINS; SEARCH
Tags OA, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 5. 4. 2016 12:25.
Abstract
A study of the effects of salt conditions on the association and dissociation of wild type p53 with different ~3 kbp long plasmid DNA substrates (supercoiled, relaxed circular and linear, containing or lacking a specific p53 binding site, p53CON) using immunoprecipitation at magnetic beads is presented. Salt concentrations above 200 mM strongly affected association of the p53 protein to any plasmid DNA substrate. Strikingly different behavior was observed when dissociation of pre-formed p53-DNA complexes in increased salt concentrations was studied. While contribution from the p53CON to the stability of the p53-DNA complexes was detected between 100 and 170 mM KCl, p53 complexes with circular DNAs (but not linear) exhibited considerable resistance towards salt treatment for KCl concentrations as high as 2 M provided that the p53 basic C-terminal DNA binding site (CTDBS) was available for DNA binding. On the contrary, when the CTDBS was blocked by antibody used for immunoprecipitation, all p53-DNA complexes were completely dissociated from the p53 protein in KCl concentrations >= 200 mM under the same conditions. These observations suggest: (a) different ways for association and dissociation of the p53-DNA complexes in the presence of the CTDBS; and (b) a critical role for a sliding mechanism, mediated by the C-terminal domain, in the dissociation process.
Links
GBP206/12/G151, research and development projectName: Centrum nových přístupů k bioanalýze a molekulární diagnostice
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