- Adaptive Stress Response to Menadione-Induced Oxidative Stress in Saccharomyces cerevisiae KNU5377
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Il-Sup Kim , Ho-Yong Sohn , Ingnyol Jin
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J. Microbiol. 2011;49(5):816-823. Published online November 9, 2011
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DOI: https://doi.org/10.1007/s12275-011-1154-6
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The molecular mechanisms involved in the ability of yeast cells to adapt and respond to oxidative stress are of great interest to the pharmaceutical, medical, food, and fermentation industries. In this study, we investigated the time-dependent, cellular redox homeostasis ability to adapt to menadione-induced oxidative stress, using biochemical and proteomic approaches in Saccharomyces cerevisiae KNU5377. Time-dependent cell viability was inversely proportional to endogenous amounts of ROS measured by a fluorescence assay with 2′,7′-dichlorofluorescin diacetate (DCFHDA), and was hypersensitive when cells were exposed to the compound for 60 min. Morphological changes, protein oxidation and lipid peroxidation were also observed. To overcome the unfavorable conditions due to the presence of menadione, yeast cells activated a variety of cell rescue proteins including antioxidant enzymes, molecular chaperones, energy-generating metabolic enzymes, and antioxidant molecules such as trehalose. Thus, these results show that menadione causes ROS generation and high accumulation of cellular ROS levels, which affects cell viability and cell morphology and there is a correlation between resistance to menadione and the high induction of cell rescue proteins after cells enter into this physiological state, which provides a clue about the complex and dynamic stress response in yeast cells.
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- Regulation of Branched-Chain, and Sulfur-Containing Amino Acid Metabolism by Glutathione during Ultradian Metabolic Oscillation of Saccharomyces cerevisiae
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Ho-Yong Sohn , Eun-Joo Kum , Gi-Seok Kwon , Ingnyol Jin , Hiroshi Kuriyama
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J. Microbiol. 2005;43(4):375-380.
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DOI: https://doi.org/2250 [pii]
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Autonomous ultradian metabolic oscillation (T~=50 min) was detected in an aerobic chemostat culture of Saccharomyces cerevisiae. A pulse injection of GSH (a reduced form of glutathione) into the culture induced a perturbation in metabolic oscillation, with respiratory inhibition caused by H_2S burst production. As the production of H_2S in the culture was controlled by different amino acids, we attempted to characterize the effects of GSH on amino acid metabolism, particularly with regard to branched chain and sulfur-containing amino acids. During stable metabolic oscillation, concentrations of intracellular glutamate, aspartate, threonine, valine, leucine, isoleucine, and cysteine were observed to oscillate with the same periods of dissolved O_2 oscillation, although the oscillation amplitudes and maximal phases were shown to differ. The methionine concentration was stably maintained at 0.05 mM. When GSH (100 uM) was injected into the culture, cellular levels of branched chain amino acids increased dramatically with continuous H_2S production, whereas the cysteine and methionine concentrations were noticeably reduced. These results indicate that GSH-dependent perturbation occurs as the result of the promotion of branched chain amino acid synthesis and an attenuation of cysteine and methionine synthesis, both of which activate the generation of H_2S. In a low sulfate medium containing 2.5 mM sulfate, the GSH injections did not result in perturbations of dissolved O_2, NAD(P)H redox oscillations without burst H_2S production. This suggests that GSH-dependent perturbation is intimately linked with the metabolism of branched-chain amino acids and H_2S generation, rather than with direct GSH-GSSG redox control.
- Identification of Two-Component Regulatory Genes Involved in o-Xylene Degradation by Rhodococcus sp. Strain DK17
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Dockyu Kim , Jong-Chan Chae , Gerben J. Zylstra , Ho-Yong Sohn , Gi-Seok Kwon , Eungbin Kim
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J. Microbiol. 2005;43(1):49-53.
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DOI: https://doi.org/2138 [pii]
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Abstract
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Putative genes for a two-component signal transduction system (akbS and akbT) were detected near the alkylbenzene-degrading operon of Rhodococcus sp. DK17. Sequence analysis indicates that AkbS possesses potential ATP-binding and histidine autophosphorylation sites in the N- and C-terminal regions, respectively, and that AkbT has a typical response regulator domain. Mutant analysis combined with RT-PCR experiments further shows that AkbS is required to induce the expression of o-xylene dioxygenase in DK17.
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