Analysis of transactivation capability and conformation of p53 temperature-dependent mutants and their reactivation by amifostine in yeast
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
17724467
DOI
10.1038/sj.onc.1210748
PII: 1210748
Knihovny.cz E-zdroje
- MeSH
- aktivace transkripce účinky léků genetika MeSH
- amifostin farmakologie MeSH
- konformace proteinů účinky léků MeSH
- lidé MeSH
- nádorový supresorový protein p53 biosyntéza chemie genetika MeSH
- radioprotektivní látky farmakologie MeSH
- Saccharomyces cerevisiae - proteiny účinky léků genetika MeSH
- substituce aminokyselin genetika MeSH
- teplota * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- amifostin MeSH
- nádorový supresorový protein p53 MeSH
- radioprotektivní látky MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- TP53 protein, human MeSH Prohlížeč
The p53 gene is often mutated during cancer development. Frequency and functional consequences of these mutations vary in different tumor types. We analysed conformation and temperature dependency of 23 partially inactivating temperature-dependent (td) p53 mutants derived from various human tumors in yeast. We found considerable differences in transactivation capabilities and discriminative character of various p53 mutants. No correlations in transactivation rates and conformations of the td p53 proteins were detected. Amifostine-induced p53 reactivation occurred only in 13 of 23 td mutants, and this effect was temperature dependent and responsive element specific. The most of the p53 mutations (10/13) reactivated by amifostine were located in the part of the p53 gene coding for hydrophobic beta-sandwich structure of the DNA-binding domain.
Citace poskytuje Crossref.org
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