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Interfacial properties of p53-DNA complexes containing various recognition elements
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SYSNO ASEP 0520366 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Interfacial properties of p53-DNA complexes containing various recognition elements Author(s) Černocká, Hana (BFU-R) RID, ORCID
Fojt, Lukáš (BFU-R) RID, ORCID
Adámik, Matěj (BFU-R) ORCID
Brázdová, Marie (BFU-R) RID, ORCID
Paleček, Emil (BFU-R) RID, ORCID
Ostatná, Veronika (BFU-R) RID, ORCIDNumber of authors 6 Article number 113300 Source Title Journal of Electroanalytical Chemistry. - : Elsevier - ISSN 1572-6657
Roč. 848, SEP 1 2019 (2019)Number of pages 7 s. Publication form Online - E Language eng - English Country CH - Switzerland Keywords dna-binding ; p53 tetramer ; nonconjugated proteins ; core domain Subject RIV CG - Electrochemistry OECD category Analytical chemistry R&D Projects GA18-18154S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support BFU-R - RVO:68081707 UT WOS 000504505400044 DOI 10.1016/j.jelechem.2019.113300 Annotation Methods which can distinguish between specific and non-specific protein interactions leading to the identification of hubs and nodes are still desired. This work shows utilization of chronopotentiometric stripping analysis in combination with a mercury electrode in the study of protein-DNA interactions at thiol-modified electrodes. The complex of tumor suppressor p53 core domain (p53CD) and DNA undergoes disintegration due to the effect of the electric field, accompanied by a remarkable increase in the electrocatalytic reduction signal. By adjusting stripping current intensities and temperature, the transition between intact and disintegrated complex reflected differences in the stabilities of sequence-specific complexes with different recognition elements. Higher stabilities of p53-DNA complexes were observed for DNA binding sites connected with cell-cycle arrest and p53 negative autoregulation, than those for DNA associated with cell apoptosis, in good concordance with electrophoretic mobility shift assay in polyacrylamide gels. These data highlight the utility of this method for studying the dynamics of surface-attached protein-DNA complexes. (C) 2019 Elsevier B.V. All rights reserved. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2020 Electronic address https://www.sciencedirect.com/science/article/pii/S1572665719305685?via%3Dihub
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