Interfacial properties of p53-DNA complexes containing various recognition elements

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00520366" target="_blank" >RIV/68081707:_____/19:00520366 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S1572665719305685?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1572665719305685?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jelechem.2019.113300" target="_blank" >10.1016/j.jelechem.2019.113300</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Interfacial properties of p53-DNA complexes containing various recognition elements

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Interfacial properties of p53-DNA complexes containing various recognition elements

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

<a href="/cs/project/GA18-18154S" target="_blank" >GA18-18154S: Nové nástroje elektrochemické analýzy proteinových interakcí s nukleovými kyselinami a proteiny nevyžadující značení</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Electroanalytical Chemistry

ISSN

1572-6657

e-ISSN

—

Svazek periodika

848

Číslo periodika v rámci svazku

SEP 1 2019

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

7

Strana od-do

113300

Kód UT WoS článku

000504505400044

EID výsledku v databázi Scopus

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