The system biology of thiol redox system in <i>Escherichia coli</i> and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis

Toledano, Michel B.; Kumar, Chitranshu; Moan, Natacha Le; Spector, Dan; Tacnet, Frédérique

doi:10.1016/j.febslet.2007.07.002

Cited by 129 publications

(123 citation statements)

References 104 publications

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“…Up-regulation of the sulfur amino acid pathway would thus result in higher levels of glutathione (which requires cysteine for its synthesis) needed for the redox response against oxidant conditions. Glutathione is the substrate for glutaredoxins, a group of thiol oxidoreductases participating in the oxidative stress response (42,43). These, together with other oxidoreductases and additional enzymes detoxifying reactive oxygen species, were induced in our study.…”

Section: Mrna Synthesis and Decay During The Yeast Oxidative Responsementioning

confidence: 95%

Comprehensive Transcriptional Analysis of the Oxidative Response in Yeast

Molina-Navarro

Castells‐Roca

Bellı́

et al. 2008

Journal of Biological Chemistry

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The oxidative stress response in Saccharomyces cerevisiae has been analyzed by parallel determination of mRNA levels and transcription rates for the entire genome. A mathematical algorithm has been adapted for a dynamic situation such as the response to stress, to calculate theoretical mRNA decay rates from the experimental data. Yeast genes have been grouped into 25 clusters according to mRNA level and transcription rate kinetics, and average mRNA decay rates have been calculated for each cluster. In most of the genes, changes in one or both experimentally determined parameters occur during the stress response. 24% of the genes are transcriptionally induced without an increase in mRNA levels. The lack of parallelism between the evolution of the mRNA amount and transcription rate predicts changes in mRNA stability during stress. Genes for ribosomal proteins and rRNA processing enzymes are abundant among those whose mRNAs are predicted to destabilize. The number of genes whose mRNAs are predicted to stabilize is lower, although some protein folding or proteasomal genes are among the latter. We have confirmed the mathematical predictions for several genes pertaining to different clusters by experimentally determining mRNA decay rates using the regulatable tetO promoter in transcriptional expression conditions not affected by the oxidative stress. This study indicates that the oxidative stress response in yeast cells is not only conditioned by gene transcription but also by the mRNA decay dynamics and that this complex response may be particularly relevant to explain the temporary down-regulation of protein synthesis occurring during stress.

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Section: Mrna Synthesis and Decay During The Yeast Oxidative Responsementioning

confidence: 95%

Comprehensive Transcriptional Analysis of the Oxidative Response in Yeast

Molina-Navarro

Castells‐Roca

Bellı́

et al. 2008

Journal of Biological Chemistry

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“…The control of H 2 O 2 -adaptive response in S. cerevisiae involves Yap1p, Skn7p and Msn2p/Msn4p (Msn2/4p) transcriptional factors ( Figure 2) [7,23,26,32,33]. Mutants deleted for YAP1 or SKN7 as well as MSN2 and MSN4 genes were found to be unable to induce most antioxidant proteins of the H 2 O 2 stimulon, indicating that they were hypersensitive to hydrogen peroxide [55][56][57][58].…”

Section: Regulation Of Global Responsementioning

confidence: 99%

“…Expression of the OxyR regulon is regulated by the transcriptional factor OxyR, which can be oxidized by hydrogen peroxide via formation of an intramolecular disulfide bond [22,25,26]. OxyR oxidation is a very rapid and sensitive process -it occurs within 30 seconds with an intracellular H 2 O 2 concentration as low as 0.1 μM [7].…”

Section: Regulation Of Global Responsementioning

confidence: 99%

Hydrogen peroxide-induced response in E. coli and S. cerevisiae: different stages of the flow of the genetic information

Semchyshyn

2009

Open Life Sciences

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Adaptation to oxidative stress is a major topic in basic and applied research. Cell response to stressful changes is realized through coordinated reorganization of gene expression. E. coli and S. cerevisiae are extremely amenable to genetic or molecular biological and biochemical approaches, which make these microorganisms suitable models to study stress response at a molecular level in prokaryotes and eukaryotes, respectively. The main focus of this review is (i) to discuss transcriptional control of global response to hydrogen peroxide in E. coli and S. cerevisiae, (ii) to summarize recent literature data on E. coli and S. cerevisiae adaptive response to oxidative stress at different stages of the flow of the genetic information: from transcription and translation to functionally active proteins and (iii) to discuss possible reasons for a lack of correlation between the expression of certain antioxidant genes at different levels of cellular organization.

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“…In addition to being a component of the amino acids cysteine and methionine, sulfur is present in reducing compounds (e.g. hydrogen sulfide and glutathione) that play an important role in maintaining the redox conditions of the bacterial cytoplasm and in detoxification of reactive oxygen species (Toledano et al, 2007). E. coli can utilize a wide range of sulfur sources, both inorganic (e.g.…”

Section: Introductionmentioning

confidence: 99%

Sulfate assimilation pathway intermediate phosphoadenosine 5′-phosphosulfate acts as a signal molecule affecting production of curli fibres in Escherichia coli

et al. 2014

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The enterobacterium Escherichia coli can utilize a variety of molecules as sulfur sources, including cysteine, sulfate, thiosulfate and organosulfonates. An intermediate of the sulfate assimilation pathway, adenosine 59-phosphosulfate (APS), also acts as a signal molecule regulating the utilization of different sulfur sources. In this work, we show that inactivation of the cysH gene, leading to accumulation of phosphoadenosine 59-phosphosulfate (PAPS), also an intermediate of the sulfate assimilation pathway, results in increased surface adhesion and cell aggregation by activating the expression of the curli-encoding csgBAC operon. In contrast, curli production was unaffected by the inactivation of any other gene belonging to the sulfate assimilation pathway. Overexpression of the cysH gene downregulated csgBAC transcription, further suggesting a link between intracellular PAPS levels and curli gene expression. In addition to curli components, the Flu, OmpX and Slp proteins were also found in increased amounts in the outer membrane compartment of the cysH mutant; deletion of the corresponding genes suggested that these proteins also contribute to surface adhesion and cell surface properties in this strain. Our results indicate that, similar to APS, PAPS also acts as a signal molecule, albeit with a distinct mechanism and role: whilst APS regulates organosulfonate utilization, PAPS would couple availability of sulfur sources to remodulation of the cell surface, as part of a more global effect on cell physiology.

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The system biology of thiol redox system in Escherichia coli and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis

Cited by 129 publications

References 104 publications

Comprehensive Transcriptional Analysis of the Oxidative Response in Yeast

Comprehensive Transcriptional Analysis of the Oxidative Response in Yeast

Hydrogen peroxide-induced response in E. coli and S. cerevisiae: different stages of the flow of the genetic information

Sulfate assimilation pathway intermediate phosphoadenosine 5′-phosphosulfate acts as a signal molecule affecting production of curli fibres in Escherichia coli

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