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Oxidative Stress Tolerance (oxidative + stress_tolerance)

Distribution by Scientific Domains
Life Sciences83%

Selected Abstracts

Role of glutathione metabolism status in the definition of some cellular parameters and oxidative stress tolerance of Saccharomyces cerevisiae cells growing as biofilms

FEMS YEAST RESEARCH, Issue 5 2008
Grégoire Gales
Abstract The resistance of Saccharomyces cerevisiae to oxidative stress (H2O2 and Cd2+) was compared in biofilms and planktonic cells, with the help of yeast mutants deleted of genes related to glutathione metabolism and oxidative stress. Biofilm-forming cells were found predominantly in the G1 stage of the cell cycle. This might explain their higher tolerance to oxidative stress and the young replicative age of these cells in an old culture. The reduced glutathione status of S. cerevisiae was affected by the growth phase and apparently plays an important role in oxidative stress tolerance in cells growing as a biofilm. [source]

JNK signaling in insulin-producing cells is required for adaptive responses to stress in Drosophila

AGING CELL, Issue 3 2009
Jason Karpac
Summary Adaptation to environmental challenges is critical for the survival of an organism. Repression of Insulin/IGF Signaling (IIS) by stress-responsive Jun-N-terminal Kinase (JNK) signaling is emerging as a conserved mechanism that allows reallocating resources from anabolic to repair processes under stress conditions. JNK activation in Insulin-producing cells (IPCs) is sufficient to repress Insulin and Insulin-like peptide (ILP) expression in rats and flies, but the significance of this interaction for adaptive responses to stress is unclear. In this study, it is shown that JNK activity in IPCs of flies is required for oxidative stress-induced repression of the Drosophila ILP2. It is found that this repression is required for growth adaptation to heat stress as well as adult oxidative stress tolerance, and that induction of stress response genes in the periphery is in part dependent on IPC-specific JNK activity. Endocrine control of IIS by JNK in IPCs is thus critical for systemic adaptation to stress. [source]

Glycinebetaine accumulation is more effective in chloroplasts than in the cytosol for protecting transgenic tomato plants against abiotic stress

PLANT CELL & ENVIRONMENT, Issue 8 2007
EUNG-JUN PARK
ABSTRACT Tomato (Lycopersicon esculentum Mill. cv. Moneymaker) plants were transformed with a gene for choline oxidase (codA) from Arthrobacter globiformis. The gene product (CODA) was targeted to the chloroplasts (Chl,codA), cytosol (Cyt,codA) or both compartments simultaneously (ChlCyt,codA). These three transgenic plant types accumulated different amounts and proportions of glycinebetaine (GB) in their chloroplasts and cytosol. Targeting CODA to either the cytosol or both compartments simultaneously increased total GB content by five- to sixfold over that measured from the chloroplast targeted lines. Accumulation of GB in codA transgenic plants was tissue dependent, with the highest levels being recorded in reproductive organs. Despite accumulating, the lowest amounts of GB, Chl,codA plants exhibited equal or higher degrees of enhanced tolerance to various abiotic stresses. This suggests that chloroplastic GB is more effective than cytosolic GB in protecting plant cells against chilling, high salt and oxidative stresses. Chloroplastic GB levels were positively correlated with the degree of oxidative stress tolerance conferred, whereas cytosolic GB showed no such a correlation. Thus, an increase in total GB content does not necessarily lead to enhanced stress tolerance, but additional accumulation of chloroplastic GB is likely to further raise the level of stress tolerance beyond what we have observed. [source]

Effects of salinity levels on proteome of Suaeda aegyptiaca leaves

PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 8 2006
Hossein Askari
Abstract Saline soils are the major problem of cultivated lands of Iran. Suaeda aegyptiaca is a salt-tolerant plant (halophytes) that grow naturally in salt-affected areas of Iran. We have employed proteomics to identify the mechanisms of salt responsiveness in leaves of S.,aegyptiaca grown under different salt concentrations. Ten-day-old plants were treated with 0, 150, 300, 450, and 600,mM NaCl. After 30,days of treatment, leaf samples were collected and analyzed using 2-D-PAGE. Out of 700,protein spots reproducible detected within replications, 102,spots showed significant response to salt treatment compared to 0,mM,NaCl. We analyzed expression pattern of salt-responsive proteins using a hierarchical and two nonhierarchical (Fuzzy ART and SOM) statistical methods and concluded that Fuzzy ART is the superior method. Forty proteins of 12,different expression groups were analyzed using LC/MS/MS. Of these, 27,protein spots were identified including proteins involved in oxidative stress tolerance, glycinebetain synthesis, cytoskeleton remodeling, photosynthesis, ATP production, protein degradation, cyanide detoxification, and chaperone activities. The expression pattern of these proteins and their possible roles in the adaptation of S.,aegyptiaca to salinity is discussed. [source]

26S proteasome regulatory particle mutants have increased oxidative stress tolerance

THE PLANT JOURNAL, Issue 1 2008
Jasmina Kurepa
Summary The 26S proteasome (26SP) is a multi-subunit, multi-catalytic protease that is responsible for most of the cytosolic and nuclear protein turnover. The 26SP is composed of two sub-particles, the 19S regulatory particle (RP) that binds and unfolds protein targets, and the 20S core particle (20SP) that degrades proteins into small peptides. Most 26SP targets are conjugated to a poly-ubiquitin (Ub) chain that serves as a degradation signal. However, some targets, such as oxidized proteins, do not require a poly-Ub tag for proteasomal degradation, and recent studies have shown that the main protease in this Ub-independent pathway is free 20SP. It is currently unknown how the ratio of 26SP- to 20SP-dependent proteolysis is controlled. Here we show that loss of function of the Arabidopsis RP subunits RPT2a, RPN10 and RPN12a leads to decreased 26SP accumulation, resulting in reduced rates of Ub-dependent proteolysis. In contrast, all three RP mutants have increased 20SP levels and thus enhanced Ub-independent protein degradation. As a consequence of this shift in proteolytic activity, mutant seedlings are hypersensitive to stresses that cause protein misfolding, and have increased tolerance to treatments that promote protein oxidation. Taken together, the data show that plant cells increase 20SP-dependent proteolysis when 26SP activity is impaired. [source]