
PSK 1 regulates expression of SOD 1 involved in oxidative stress tolerance in yeast
Author(s) -
Huang Meixian,
Xu Qinghong,
Mitsui Kazuhiro,
Xu Zhaojun
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12329
Subject(s) - sod1 , mutant , biology , yeast , wild type , pas domain , oxidative stress , biochemistry , reactive oxygen species , sod2 , superoxide dismutase , microbiology and biotechnology , protein kinase a , kinase , gene , transcription factor
The P er– ARNT – S im ( PAS ) domain serine/threonine kinase PAS kinase is involved in energy flux and protein synthesis. In yeast, PSK 1 and PSK 2 are two partially redundant PASK homologs. We recently generated PSK 2 deletion mutant and showed that P sk2 acts as a nutrient‐sensing protein kinase to modulate U ltradian clock‐coupled respiratory oscillation in yeast. Here, we show that deletion of PSK 1 increased the sensitivity of yeast cells to oxidative stress ( H 2 O 2 treatment) and partially inhibited cell growth; however, the growth of the PSK2 ‐deleted mutant was similar to that of the wild type. Superoxide dismutase‐1 ( SOD 1 ) m RNA and protein levels were lower in PSK 1 ‐deletion mutant than the wild type. The m RNA levels of stress response genes CTT 1 , HSP 104 , ATH 1 , NTH 1 and SOD 2 were similar in both the PSK 1 ‐deleted mutant and wild‐type yeast. Furthermore, intracellular accumulation of reactive oxygen species ( ROS ) was noted in PSK 1 ‐deleted mutant. These results suggest that PSK 1 induces SOD 1 expression to protect against oxidative stress in yeast.