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Updated: May 8, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
Enhanced redox factor 1 (REF1)-modulated p53 stabilization and JNK1 dissociation in response to selenomethionine
Hwa Jin Jung1, Hye Lim Kim, Young Rok Seo
1Department of Life Science, Dongguk University, 30 Pildong-ro 1-gil, Jung-gu, Seoul 100-715, Republic of Korea, seoyr@dongguk.edu.
Aim:
p53 is reportedly activated without any genotoxicity through redox modulation of redox factor 1 (REF1). REF1 is documented to modulate the redox status under selenomethionine (SeMet). In this study, we investigated the mechanism of p53 stabilization by SeMet.
Materials And Methods:
We mainly used ubiquitination assay and immunoprecipitation to determine the potential role of REF1 and c-jun N-terminal kinase 1 (JNK) in modulation of p53 stabilization by SeMet.
Results:
The amount of ubiquitinated p53 decreased significantly under SeMet treatment, suggesting that SeMet might inhibit the proteasome-dependent degradation of p53. In addition, we observed that JNK was considerably associated with p53 in REF1 siRNA-treated cells, implying a possible role for SeMet-induced REF1 activity in modulation of the interaction between JNK and p53 via changes in p53 redox status.
Conclusion:
Our results suggest that the alternate mechanism of p53 stabilization by SeMet might provide an important clue in elucidating the molecular mechanism of chemopreventative compounds against various oxidative stresses.
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