On the role of glutathione in the transport of amino acid in the yeast <i>Saccharomyces cerevisiae</i>: contradictory results

Jaspers, Charles; Penninckx, Michel

doi:10.1016/0014-5793(81)80423-1

Cited by 16 publications

(7 citation statements)

References 18 publications

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“…al., 1980) was later contradicted (Robins & Davies, 1981;Jaspers & Penninckx, 1981;Payne & Payne, 1984). Here we show that nitrogen starvation induced a migration of more than 90% of GSH towards the central vacuole (tonoplast) of the yeast cell.…”

Section: Abbreviations: Bso Buthionine-(sr)-sulphoximine; 7-gcsmentioning

confidence: 71%

“…In contrast, no clear physiological function was attributed to the repressive effect of the ammonium ion. A possible role for γ-GT in the bulk transport of amino acids by S. cerevisiae (Penninckx et al, 1980) was later contradicted (Robins & Davies, 1981; Jaspers & Penninckx, 1981; Payne & Payne, 1984). Here we show that nitrogen starvation induced a migration of more than 90％ of GSH towards the central vacuole (tonoplast) of the yeast cell.…”

Section: Introductionmentioning

confidence: 99%

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An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae

1997

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When the yeast Saccharomyces cerevisiae E1278b was starved for nitrogen, the total glutathione (GSH) pool increased from 7 to 17 nmol (mg dry wt)-' during the first 2 h and then declined. More than 90% of the total GSH shifted towards the central vacuole during this time. This transient stimulation was not observed in the presence of buthionine-(S,R)-sulphoximine (BSO), a specific transition-state-analogue inhibitor of y-glutamylcysteine synthase (y-GCS), nor in a mutant strain deficient in this enzyme. y-Glutamyltranspeptidase (y-GT), a vacuolar enzyme responsible for the initial step of GSH degradation, was derepressed during nitrogen starvation. This mechanism can apparently enable the starved yeast cell to use the constituent amino acids from GSH which accumulate in the vacuole to satisfy its growth requirements for nitrogen.Keywords : yeast, glutathione, y-glutamyltranspeptidase, nitrogen starvation, vacuoles INTRODUCTIONGlutathione (GSH; L-y-glutamyl-L-cysteinylglycine) is present in high concentration in most living cells from micro-organisms to man, and has been shown to play numerous roles, in particular in the yeast Saccharomyces cerevisiae, where it may account for 1 O h of the cell dry weight (Penninckx & Elskens, 1993). A role of GSH as an endogenous sulphur source in S. cerevisiae has previously been shown (Elskens et al., 1991). In this yeast, GSH catabolism appears to be mediated by yglut am y 1 tr an spep t i d a se (y-G T ) and cyst ein y lg 1 y ci ne dipeptidase, and leads to the formation of glutamate, cysteine and glycine (Jaspers et af., 1985). Yeast y-GT biosynthesis was found to be regulated by at least two apparently distinct pathways involving, respectively, repression by ammonium ion (Penninckx et al., 1980) and GSH (Elskens et al., 1991). Repression of p G T by GSH is related to the sulphur storage function of GSH (Elskens et al., 1991). In contrast, no clear physiological function was attributed to the repressive effect of the ammonium ion. A possible role for y-GT in the bulk transport of amino acids by S. cerevisiae . Here we show that nitrogen starvation induced a migration of more than 90% of GSH towards the central vacuole (tonoplast) of the yeast cell. This migration was accompanied by a de novo synthesis of the tripeptide and a derepression of y-GT. GSH that had accumulated in the central vacuole was further degraded and seems to play the role of a reservoir to provide the yeast cell with amino acids for subsequent growth requirements. METHODSStrains. The wild-type strain C1278b (MATa), was described by Grenson et al. (1966) and obtained from the Laboratoire de Microbiologie de 1'Universite libre de Bruxelles. The GSHdeficient mutant (gshA-2) yeast strain was from our laboratory (Elskens et al., 1991). On: Thu, 04 Apr 2019 13:57:33 K. M E H D I a n d M. J. P E N N I N C K X 10 mM (NH,),SO, as the nitrogen source (minimal medium) were harvested at 0-4-0.5 mg dry wt ml-' by rapid Millipore filtration (0.45 pm HAWP), washed twice with SBM and transferred to the same medium.Enzyme...

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Section: Abbreviations: Bso Buthionine-(sr)-sulphoximine; 7-gcsmentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae

1997

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“…Expectedly, both the promoted oxidative stress and impaired energy metabolism have several negative effects on HUVECs, in which protein synthesis block is the most prominent one. As previously reported, GSH participates in many metabolic and biochemical reactions such as DNA synthesis and repair, protein synthesis [38], amino acid transport [39], and enzyme activation [40]. The depletion of GSH caused by promoted oxidative stress could ultimately retard protein synthesis.…”

Section: Blocked Protein Synthesis During Cellular Senescencementioning

confidence: 89%

NMR-based metabonomic analysis of HUVEC cells during replicative senescence

Lin

Jiang

et al. 2020

Aging

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Cellular senescence is a physiological process reacting to stimuli, in which cells enter a state of irreversible growth arrest in response to adverse consequences associated with metabolic disorders. Molecular mechanisms underlying the progression of cellular senescence remain unclear. Here, we established a replicative senescence model of human umbilical vein endothelial cells (HUVEC) from passage 3 (P3) to 18 (P18), and performed biochemical characterizations and NMR-based metabolomic analyses. The cellular senescence degree advanced as the cells were sequentially passaged in vitro, and cellular metabolic profiles were gradually altered. Totally, 8, 16, 21 and 19 significant metabolites were primarily changed in the P6, P10, P14 and P18 cells compared with the P3 cells, respectively. These metabolites were mainly involved in 14 significantly altered metabolic pathways. Furthermore, we observed taurine retarded oxidative damage resulting from senescence. In the case of energy deficiency, HUVECs metabolized neutral amino acids to replenish energy, thus increased glutamine, aspartate and asparagine at the early stages of cellular senescence but decreased them at the later stages. Our results indicate that cellular replicative senescence is closely associated with promoted oxidative stress, impaired energy metabolism and blocked protein synthesis. This work may provide mechanistic understanding of the progression of cellular senescence.

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“…The physiological role of yeast transpeptidation reactions is not well understood. y-GT and GSH were initially thought to be involved in the bulk absorption of amino acids by S. cerevisiae, but these claims have been contradicted (Robins & Davies, 1981;Jaspers & Penninckx, 1981;Payne & Payne, 1984). In the course of an investigation into the biochemical characterization of GSH-deficient yeast mutants, we observed that these mutants showed a derepression of y-GT.…”

Section: Introductionmentioning

confidence: 91%

Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae

Elskens

Jaspers

Penninckx

1991

Journal of General Microbiology

106

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Glutathione-deficient mutants (@A) of the yeast Saccharomyces cerevisiae, impaired in the first step of glutathione (GSH) biosynthesis were studied with respect to the regulation of enzymes involved in GSH catabolism and cysteine biosynthesis. Striking differences were observed in the content of the sulphur amino acids when gshA mutants were compared to wild-type strains growing on the same minimal medium. Furthermore, all mutants examined showed a derepression of y-glutamyltranspeptidase (y-GT), the enzyme initiating GSH degradation. However, y-cystathionase and cysteine synthase were unaffected by the GSH deficiency as long as the nutrient sulphate source was not exhausted. The results suggest that the mutants are probably not impaired in the sulphate assimilation pathway, but that the y-glutamyl cycle could play a leading role in the regulation of the sulphur fluxes. Studies of enzyme regulation showed that the derepression of y-GT observed in thegshA strains was most probably due to an alteration of the thiol status. The effectors governing the biosynthesis of cysteine synthase and ycystathionase seemed different from those playing a role in y-GT regulation and it was only under conditions of total sulphate deprivation that all these enzymes were derepressed. As a consequence the endogenous pool of GSH was used in the synthesis of cysteine. GSH might, therefore, fulfil the role of a storage compound.

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On the role of glutathione in the transport of amino acid in the yeast Saccharomyces cerevisiae: contradictory results

Cited by 16 publications

References 18 publications

An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae

An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae

NMR-based metabonomic analysis of HUVEC cells during replicative senescence

Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae

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