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

J 2001

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

KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ a Viktor BRABEC

Základní údaje

Originální název

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

Autoři

KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ a Viktor BRABEC

Vydání

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. 2001, 0021-9258

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 7.258

Kód RIV

RIV/00216224:14310/01:00004213

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

DNA; p53; protinádorová aktivita; interakce; cisplatina

Štítky

cisplatina, DNA, interakce, p53, protinádorová aktivita

Změněno: 25. 5. 2001 15:16, prof. RNDr. Viktor Brabec, DrSc.

Anotace

V originále

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 to mean 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 results also demonstrate an increase of the binding affinity of p53 to DNA lacking the consensus sequence and modified by cisplatin, but not by transplatin.

Návaznosti

GA305/99/0695, projekt VaV

Název: Ovlivnění konformace DNA protinádorově účinnými komplexy kovů. Vztah k vývoji nových cytostatik.

Citovat

KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ a Viktor BRABEC. Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol., 2001, roč. 276, č. 19, s. 16064-16069. ISSN 0021-9258.

@article{362474,
   author = {Kašpárková, Jana and Pospíšilová, Šárka and Brabec, Viktor},
   article_location = {Bethesda, USA},
   article_number = {19},
   keywords = {DNA; p53; protinádorová aktivita; interakce; cisplatina},
   language = {eng},
   issn = {0021-9258},
   journal = {Journal of Biological Chemistry},
   title = {Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53},
   volume = {276},
   year = {2001}
}

TY  - JOUR
ID  - 362474
AU  - Kašpárková, Jana - Pospíšilová, Šárka - Brabec, Viktor
PY  - 2001
TI  - Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53
JF  - Journal of Biological Chemistry
VL  - 276
IS  - 19
SP  - 16064
EP  - 16064
PB  - Amer. Soc. Biochem. Mol.
SN  - 00219258
KW  - DNA
KW  - p53
KW  - protinádorová aktivita
KW  - interakce
KW  - cisplatina
N2  - 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 to mean 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 results also demonstrate an increase of the binding affinity of p53 to DNA lacking the consensus sequence and modified by cisplatin, but not by transplatin.
ER  -

KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ a Viktor BRABEC. Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol., 2001, roč.~276, č.~19, s.~16064-16069. ISSN~0021-9258.

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