Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione.

@article{Merwin2002ReporterGT,
  title={Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione.},
  author={Jason R Merwin and Debbie J. Mustacich and Eric G. D. Muller and George D. Pearson and Gary Frederic Merrill},
  journal={Carcinogenesis},
  year={2002},
  volume={23 10},
  pages={1609-15}
}
Reporter gene transactivation by human p53 is compromised in S. cerevisiae lacking the TRR1 gene encoding thioredoxin reductase. The basis for p53 inhibition was investigated by measuring the redox state of thioredoxin and glutathione in wild-type and Deltatrr1 yeast. The Deltatrr1 mutation affected the redox state of both molecules. About 34% of thioredoxin was in the disulfide form in wild-type yeast and increased to 70% in Deltatrr1 yeast. About 18% of glutathione was in the GSSG form in… CONTINUE READING
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Thioredoxin - dependent redox regulation of p 53 - mediated p 21 activation

  • M. Ueno, R. J. Masutani, A. Arai
  • 1999

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