Detailed Information on Publication Record
2001
Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53
KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ and Viktor BRABECBasic information
Original name
Different recognition of DNA modified by antitumor cisplatin and its clinically ineffective trans isomer by tumor suppressor protein p53
Authors
KAŠPÁRKOVÁ, Jana, Šárka POSPÍŠILOVÁ and Viktor BRABEC
Edition
Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. 2001, 0021-9258
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10610 Biophysics
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 7.258
RIV identification code
RIV/00216224:14310/01:00004213
Organization unit
Faculty of Science
Keywords in English
DNA; p53; protinádorová aktivita; interakce; cisplatina
Tags
Změněno: 25/5/2001 15:16, prof. RNDr. Viktor Brabec, DrSc.
Abstract
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.
Links
| GA305/99/0695, research and development project |
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