Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F01%3A00004213" target="_blank" >RIV/00216224:14310/01:00004213 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/01:17013022

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53

Popis výsledku v původním jazyce

DNA binding activity of p53 protein is crucial for its tumor suppressor function. DNA interactions of active wild-type human p53 protein with DNA fragments and oligodeoxyribonucleotide duplexes modified by antitumor cisplatin and its clinically ineffective trans isomer (transplatin) was investigated by using gel-mobility-shift assay. It was found that DNA adducts of cisplatin reduced binding affinity of the consensus DNA sequence to p53 whereas transplatin adducts do not. This result was interpreted tomean that the precise steric fit required for formation and stability of the tetrameric complex of p53 with the consensus sequence cannot be attained as a consequence of severe conformational perturbances induced in DNA by cisplatin adducts. The resultsalso demonstrate an increase of the binding affinity of p53 to DNA lacking the consensus sequence and modified by cisplatin, but not by transplatin.

Název v anglickém jazyce

Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53

Popis výsledku anglicky

DNA binding activity of p53 protein is crucial for its tumor suppressor function. DNA interactions of active wild-type human p53 protein with DNA fragments and oligodeoxyribonucleotide duplexes modified by antitumor cisplatin and its clinically ineffective trans isomer (transplatin) was investigated by using gel-mobility-shift assay. It was found that DNA adducts of cisplatin reduced binding affinity of the consensus DNA sequence to p53 whereas transplatin adducts do not. This result was interpreted tomean that the precise steric fit required for formation and stability of the tetrameric complex of p53 with the consensus sequence cannot be attained as a consequence of severe conformational perturbances induced in DNA by cisplatin adducts. The resultsalso demonstrate an increase of the binding affinity of p53 to DNA lacking the consensus sequence and modified by cisplatin, but not by transplatin.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2001

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

276

Číslo periodika v rámci svazku

19

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

6

Strana od-do

16064

Kód UT WoS článku

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EID výsledku v databázi Scopus

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