Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368

Pébay, Mireille; Holl, Anne-Catherine; Simonet, Jean-Marc; Decaris, Bernard

doi:10.1016/0923-2508(96)80283-x

Cited by 23 publications

(16 citation statements)

References 38 publications

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“…The fact that some clostridiales have the ability to synthesize GSH whereas others do not suggests that the genes for GSH metabolism may have been acquired late in the evolutionary process, perhaps by horizontal gene transfer (13,14,24) from a host with GSH synthesis capacity colonized by these bacteria. It is pertinent to note that a GSH reductase activity has been found in extracts of Streptococcus thermophilus and a disulfide reductase gene from this organism has been shown to have substantial sequence identity to the GSH reductase from Escherichia coli (22).…”

Section: Discussionmentioning

confidence: 99%

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

et al. 1996

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Mycothiol [2-(N-acetylcysteinyl)amido-2-deoxy-␣-D-glucopyranosyl-(131)-myo-inositol] (MSH. Since this novel thiol is more resistant than glutathione to heavy-metal ion-catalyzed oxidation, it seems likely to be the antioxidant thiol used by aerobic gram-positive bacteria that do not produce glutathione (GSH). In the present study we sought to define the spectrum of organisms that produce MSH. GSH was absent in all actinomycetes and some of the other gram-positive bacteria studied. Surprisingly, the streptococci and enterococci contained GSH, and some strains appeared to synthesize it rather than import it from the growth medium. MSH was found at significant levels in most actinomycetes examined. Among the actinobacteria four Micrococcus species produced MSH, but MSH was not found in representatives of the Arthrobacter, Agromyces, or Actinomyces genera. Of the nocardioforms examined, Nocardia, Rhodococcus, and Mycobacteria spp. all produced MSH. In addition to the established production of MSH by streptomycetes, we found that Micromonospora, Actinomadura, and Nocardiopsis spp. also synthesized MSH. Mycothiol production was not detected in Propionibacterium acnes or in representative species of the Listeria, Staphylococcus, Streptococcus, Enterococcus, Bacillus, and Clostridium genera. Examination of representatives of the cyanobacteria, purple bacteria, and spirochetes also gave negative results, as did tests of rat liver, bonito, Candida albicans, Neurospora crassa, and spinach leaves. The results, which indicate that MSH production is restricted to the actinomycetes, could have significant implications for the detection and treatment of infections with actinomycetes, especially those caused by mycobacteria.

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Section: Discussionmentioning

confidence: 99%

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

et al. 1996

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“…The first report of GR in lactic acid bacteria appeared in 1995, by Pebay et al (35), providing new data concerning lactic acid bacterium responses to oxidative stress. Since the principal thiol-disulfide redox buffer in the cytoplasm of bacteria is thought to be glutathione (46), GR is probably important for maintaining the redox potential at a low level for protection of thiol-containing proteins against oxidative stress.…”

Section: Discussionmentioning

confidence: 99%

Effect of Adaptation to Ethanol on Cytoplasmic and Membrane Protein Profiles of Oenococcus oeni

Silveira

Baumgärtner

Rombouts

et al. 2004

Appl Environ Microbiol

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The practical application of commercial malolactic starter cultures of Oenococcus oeni surviving direct inoculation in wine requires insight into mechanisms of ethanol toxicity and of acquired ethanol tolerance in this organism. Therefore, the site-specific location of proteins involved in ethanol adaptation, including cytoplasmic, membrane-associated, and integral membrane proteins, was investigated. Ethanol triggers alterations in protein patterns of O. oeni cells stressed with 12% ethanol for 1 h and those of cells grown in the presence of 8% ethanol. Levels of inosine-5-monophosphate dehydrogenase and phosphogluconate dehydrogenase, which generate reduced nicotinamide nucleotides, were decreased during growth in the presence of ethanol, while glutathione reductase, which consumes NADPH, was induced, suggesting that maintenance of the redox balance plays an important role in ethanol adaptation. Phosphoenolpyruvate:mannose phosphotransferase system (PTS) components of mannose PTS, including the phosphocarrier protein HPr and EII Man , were lacking in ethanol-adapted cells, providing strong evidence that mannose PTS is absent in ethanoladapted cells, and this represents a metabolic advantage to O. oeni cells during malolactic fermentation. In cells grown in the presence of ethanol, a large increase in the number of membrane-associated proteins was observed. Interestingly, two of these proteins, dTDT-glucose-4,6-dehydratase and D-alanine:D-alanine ligase, are known to be involved in cell wall biosynthesis. Using a proteomic approach, we provide evidence for an active ethanol adaptation response of O. oeni at the cytoplasmic and membrane protein levels.

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“…Streptococci harbor GshRs that enable the cells to create a reducing environment and which are overexpressed during aerobic growth (26,37,49). Some strains of L. lactis accumulate glutathione in response to aerobic conditions (19).…”

Section: Presence Of Gshr Bmentioning

confidence: 99%

“…Streptococcus mutans possesses a sulfhydryl uptake system (37). GshRs were characterized from Streptococcus thermophilus CNRZ368 (26) and Enterococcus faecalis (25). In Lactococcus lactis, the increased accumulation of GSH under aerobic conditions was interpreted as a regulatory mechanism that protects L. lactis cells against oxidative stress (19).…”

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confidence: 99%

Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451 ^T : Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs

Jänsch

Korakli

Vogel

et al. 2007

Appl Environ Microbiol

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The effect of the glutathione reductase (GshR) activity of Lactobacillus sanfranciscensis DSM20451 T on the thiol levels in fermented sourdoughs was determined, and the oxygen tolerance of the strain was also determined. The gshR gene coding for a putative GshR was sequenced and inactivated by single-crossover integration to yield strain L. sanfranciscensis DSM20451 T ⌬gshR. The gene disruption was verified by sequencing the truncated gshR and surrounding regions on the chromosome. The gshR activity of L. sanfranciscensis DSM20451 T ⌬gshR was strongly reduced compared to that of the wild-type strain, demonstrating that gshR indeed encodes an active GshR enzyme. The thiol levels in wheat doughs fermented with L. sanfranciscensis DSM20451 increased from 9 M to 10.5 M sulfhydryl/g of dough during a 24-h sourdough fermentation, but in sourdoughs fermented with L. sanfranciscensis DSM20451 T ⌬gshR and in chemically acidified doughs, the thiol levels decreased to 6.5 to 6.8 M sulfhydryl/g of dough. Remarkably, the GshR-negative strains Lactobacillus pontis LTH2587 and Lactobacillus reuteri BR11 exerted effects on thiol levels in dough comparable to those of L. sanfranciscensis. In addition to the effect on thiol levels in sourdough, the loss of GshR activity in L. sanfranciscensis DSM20451 T ⌬gshR resulted in a loss of oxygen tolerance. The gshR mutant strain exhibited a strongly decreased aerobic growth rate on modified MRS medium compared to either the growth rate under anaerobic conditions or that of the wild-type strain, and aerobic growth was restored by the addition of cysteine. Moreover, the gshR mutant strain was more sensitive to the superoxide-generating agent paraquat. Reduced glutathione (␥-GluCysGly [GSH]) and oxidized glutathione (GSSG) are both naturally occurring in wheat flour (11,17). These sulfhydryl compounds are capable of undergoing a disulfide-sulfhydryl interchange with other low-molecular-weight thiol compounds, as well as gluten proteins, resulting in the cleavage or reformation of disulfide bonds in wheat dough (10). The formation of the glutenin macropolymer in wheat doughs, which determines dough rheology and gas retention and, thus, bread volume and texture, is dependent on intermolecular disulfide bonds between glutenin proteins (10, 47). Oxidizing or reducing agents that influence the thiol exchange reactions between GSH and gluten proteins are therefore important components of baking improvers to standardize and to control dough rheology and bread texture in wheat baking.It was recently shown that Lactobacillus sanfranciscensis increases the levels of low-molecular-weight thiol components, as well as thiol levels, in gluten proteins during sourdough fermentation (43). This reduction of disulfide bonds by L. sanfranciscensis, in addition to the pH-dependent activities of cereal proteases, may determine the gluten quality. The effect of L. sanfranciscensis on disulfide exchange reactions in wheat doughs was attributed to the glutathione reductase (GshR) activity of this organism (43).

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Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368

Cited by 23 publications

References 38 publications

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

Effect of Adaptation to Ethanol on Cytoplasmic and Membrane Protein Profiles of Oenococcus oeni

Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451 ^T : Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs

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Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368

Cited by 23 publications

References 38 publications

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

Effect of Adaptation to Ethanol on Cytoplasmic and Membrane Protein Profiles of Oenococcus oeni

Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451 T : Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs

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Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451 ^T : Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs