Journal Article
- Identification of trehalose as a compatible solute in different species of acidophilic bacteria
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Pedro A. Galleguillos , Barry M. Grail , Kevin B. Hallberg , Cecilia S. Demergasso , D. Barrie Johnson
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J. Microbiol. 2018;56(10):727-733. Published online September 28, 2018
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DOI: https://doi.org/10.1007/s12275-018-8176-2
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Abstract
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The major industrial heap bioleaching processes are located
in desert regions (mainly Chile and Australia) where fresh
water is scarce and the use of resources with low water activity
becomes an attractive alternative. However, in spite
of the importance of the microbial populations involved in
these processes, little is known about their response or adaptation
to osmotic stress. In order to investigate the response
to osmotic stress in these microorganisms, six species of acidophilic
bacteria were grown at elevated osmotic strength in
liquid media, and the compatible solutes synthesised were
identified using ion chromatography and MALDI-TOF mass
spectrometry. Trehalose was identified as one of, or the sole,
compatible solute in all species and strains, apart from Acidithiobacillus
thiooxidans where glucose and proline levels
increased at elevated osmotic potentials. Several other potential
compatible solutes were tentatively identified by MALDITOF
analysis. The same compatible solutes were produced
by these bacteria regardless of the salt used to produce the osmotic
stress. The results correlate with data from sequenced
genomes which confirm that many chemolithotrophic and
heterotrophic acidophiles possess genes for trehalose synthesis.
This is the first report to identify and quantify compatible
solutes in acidophilic bacteria that have important
roles in biomining technologies.
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Citations
Citations to this article as recorded by

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Research Support, Non-U.S. Gov'ts
- 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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Abstract
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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.
- Heat Shock Causes Oxidative Stress and Induces a Variety of Cell Rescue Proteins in Saccharomyces cerevisiae KNU5377
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Il-Sup Kim , Hye-Youn Moon , Hae-Sun Yun , Ingnyol Jin
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J. Microbiol. 2006;44(5):492-501.
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DOI: https://doi.org/2449 [pii]
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Abstract
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In this study, we attempted to characterize the physiological response to oxidative stress by heat shock in Saccharomyces cerevisiae KNU5377 (KNU5377) that ferments at a temperature of 40°C. The KNU5377 strain evidenced a very similar growth rate at 40°C as was recorded under normal conditions. Unlike the laboratory strains of S. cerevisiae, the cell viability of KNU5377 was affected slightly under 2 hours of heat stress conditions at 43°C. KNU5377 evidenced a time-dependent increase in hydroperoxide levels, carbonyl contents, and malondialdehyde (MDA), which increased in the expression of a variety of cell rescue proteins containing Hsp104p, Ssap, Hsp30p, Sod1p, catalase, glutathione reductase, G6PDH, thioredoxin, thioredoxin peroxidase (Tsa1p), Adhp, Aldp, trehalose and glycogen at high temperature. Pma1/2p, Hsp90p and H+-ATPase expression levels were reduced as the result of exposure to heat shock. With regard to cellular fatty acid composition, levels of unsaturated fatty acids (USFAs) were increased significantly at high temperatures (43°C), and this was particularly true of oleic acid (C18:1). The results of this study indicated that oxidative stress as the result of heat shock may induce a more profound stimulation of trehalose, antioxidant enzymes, and heat shock proteins, as well as an increase in the USFAs ratios. This might contribute to cellular protective functions for the maintenance of cellular homeostasis, and may also contribute to membrane fluidity.