scholarly journals Protein aggregation and membrane lipid modifications under lactic acid stress in wild type and OPI1 deleted Saccharomyces cerevisiae strains

2016 ◽  
Vol 15 (1) ◽  
Author(s):  
Nadia Maria Berterame ◽  
Danilo Porro ◽  
Diletta Ami ◽  
Paola Branduardi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Protein Aggregation ◽  
Acid Stress ◽  
Membrane Lipid ◽  
Wild Type ◽  
Lipid Modifications

Regulation of basal and induced levels of the MEL1 transcript in Saccharomyces cerevisiae

1984 ◽  
Vol 4 (7) ◽  
pp. 1238-1245
Author(s):  
M A Post-Beittenmiller ◽  
R W Hamilton ◽  
J E Hopper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Carbon Sources ◽  
Regulatory Proteins ◽  
Northern Hybridization ◽  
Transcriptional Expression ◽  
Wild Type ◽  
Naturally Occurring ◽  
Alpha Galactosidase ◽  
In Cells

The MEL1 gene in Saccharomyces cerevisiae is required for the production of alpha-galactosidase and for the catabolism of melibiose. Production of alpha-galactosidase is induced by galactose or melibiose and repressed by glucose. Inducibility is controlled by the positive and negative regulatory proteins GAL4 and GAL80, respectively. We have cloned the MEL1 gene to study its transcriptional expression and regulation. Evidence is presented that the MEL1 gene encodes alpha-galactosidase and that mel0 is a naturally occurring allele which lacks the alpha-galactosidase-coding sequences. RNAs prepared from wild-type cells and from cells carrying either the noninducible gal4-2 or GAL80S-100 allele grown on three different carbon sources were examined by Northern hybridization analyses. In wild-type cells under noninducing conditions, such as growth on glycerol-lactic acid, the MEL1 transcript was detected at a basal level which was 1 to 2% of the fully induced level. The basal level of expression was diminished in cells carrying the gal4-2 mutant allele but not in cells carrying the GAL80S-100 allele. The basal and induced RNA levels are repressed by glucose. Size determinations of the MEL1 transcripts detected in glycerol-lactic acid- and galactose-grown cells provided no evidence for two distinct transcripts.

scholarly journals Nuclear Localization of Haa1, Which Is Linked to Its Phosphorylation Status, Mediates Lactic Acid Tolerance in Saccharomyces cerevisiae

2014 ◽  
Vol 80 (11) ◽  
pp. 3488-3495 ◽  
Author(s):  
Minetaka Sugiyama ◽  
Shin-Pei Akase ◽  
Ryota Nakanishi ◽  
Hitoshi Horie ◽  
Yoshinobu Kaneko ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Subcellular Localization ◽  
Target Genes ◽  
Acid Stress ◽  
Acid Tolerance ◽  
Acid Resistance ◽  
Nuclear Accumulation ◽  
Content Type ◽  
Adaptation Response

ABSTRACTImprovement of the lactic acid resistance of the yeastSaccharomyces cerevisiaeis important for the application of the yeast in industrial production of lactic acid from renewable resources. However, we still do not know the precise mechanisms of the lactic acid adaptation response in yeast and, consequently, lack effective approaches for improving its lactic acid tolerance. To enhance our understanding of the adaptation response, we screened forS. cerevisiaegenes that confer enhanced lactic acid resistance when present in multiple copies and identified the transcriptional factor Haa1 as conferring resistance to toxic levels of lactic acid when overexpressed. The enhanced tolerance probably results from increased expression of its target genes. When cells that expressed Haa1 only from the endogenous promoter were exposed to lactic acid stress, the main subcellular localization of Haa1 changed from the cytoplasm to the nucleus within 5 min. This nuclear accumulation induced upregulation of the Haa1 target genesYGP1,GPG1, andSPI1, while the degree of Haa1 phosphorylation observed under lactic acid-free conditions decreased. Disruption of the exportin geneMSN5led to accumulation of Haa1 in the nucleus even when no lactic acid was present. Since Msn5 was reported to interact with Haa1 and preferentially exports phosphorylated cargo proteins, our results suggest that regulation of the subcellular localization of Haa1, together with alteration of its phosphorylation status, mediates the adaptation to lactic acid stress in yeast.

scholarly journals Methylselenol Produced In Vivo from Methylseleninic Acid or Dimethyl Diselenide Induces Toxic Protein Aggregation in Saccharomyces cerevisiae

2021 ◽  
Vol 22 (5) ◽  
pp. 2241
Author(s):  
Marc Dauplais ◽  
Katarzyna Bierla ◽  
Coralie Maizeray ◽  
Roxane Lestini ◽  
Ryszard Lobinski ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Aggregation ◽  
Thioredoxin Reductase ◽  
Wild Type ◽  
Toxic Protein ◽  
Methylseleninic Acid ◽  
Dimethyl Diselenide

Methylselenol (MeSeH) has been suggested to be a critical metabolite for anticancer activity of selenium, although the mechanisms underlying its activity remain to be fully established. The aim of this study was to identify metabolic pathways of MeSeH in Saccharomyces cerevisiae to decipher the mechanism of its toxicity. We first investigated in vitro the formation of MeSeH from methylseleninic acid (MSeA) or dimethyldiselenide. Determination of the equilibrium and rate constants of the reactions between glutathione (GSH) and these MeSeH precursors indicates that in the conditions that prevail in vivo, GSH can reduce the major part of MSeA or dimethyldiselenide into MeSeH. MeSeH can also be enzymatically produced by glutathione reductase or thioredoxin/thioredoxin reductase. Studies on the toxicity of MeSeH precursors (MSeA, dimethyldiselenide or a mixture of MSeA and GSH) in S.cerevisiae revealed that cytotoxicity and selenomethionine content were severely reduced in a met17 mutant devoid of O-acetylhomoserine sulfhydrylase. This suggests conversion of MeSeH into selenomethionine by this enzyme. Protein aggregation was observed in wild-type but not in met17 cells. Altogether, our findings support the view that MeSeH is toxic in S. cerevisiae because it is metabolized into selenomethionine which, in turn, induces toxic protein aggregation.

Caractéristiques d'un mutant homothallique de Saccharomyces cerevisiae Hansen

1971 ◽  
Vol 17 (3) ◽  
pp. 425-428
Author(s):  
A. Arnaud ◽  
Françoise Vezinhet ◽  
P. Galzy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Vegetative Growth ◽  
Nitrous Acid ◽  
Solid Medium ◽  
Wild Strain ◽  
Wild Type

Through mutagenesis by nitrous acid a mutant was obtained which differed from the wild strain by two independent characters. The mutant gave smooth colonies on a solid medium containing lactic acid; the wild type yielded rough colonies on the same medium. The smooth colony character was unstable during vegetative growth. The mutant was homothallic. This character was stable during vegetative growth but it was not segregated through meïosis. This mutation inducing homothallism is not controlled by a gene.

scholarly journals Impaired Cutinase Secretion in Saccharomyces cerevisiae Induces Irregular Endoplasmic Reticulum (ER) Membrane Proliferation, Oxidative Stress, and ER-Associated Degradation

2002 ◽  
Vol 68 (5) ◽  
pp. 2155-2160 ◽  
Author(s):  
C. M. J. Sagt ◽  
W. H. Müller ◽  
L. van der Heide ◽  
J. Boonstra ◽  
A. J. Verkleij ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Protein Aggregation ◽  
Fold Increase ◽  
Proteasomal Degradation ◽  
Wild Type ◽  
Unfolded Protein ◽  
Protein Response ◽  
And Oxidative Stress

ABSTRACT Impaired secretion of the hydrophobic CY028 cutinase invokes an unfolded protein response (UPR) in Saccharomyces cerevisiae cells. Here we show that the UPR in CY028-expressing S. cerevisiae cells is manifested as an aberrant morphology of the endoplasmic reticulum (ER) and as extensive membrane proliferation compared to the ER morphology and membrane proliferation of wild-type CY000-producing S. cerevisiae cells. In addition, we observed oxidative stress, which resulted in a 21-fold increase in carbonylated proteins in the CY028-producing S. cerevisiae cells. Moreover, CY028-producing S. cerevisiae cells use proteasomal degradation to reduce the amount of accumulated CY028 cutinase, thereby attenuating the stress invoked by CY028 cutinase expression. This proteasomal degradation occurs within minutes and is characteristic of ER-associated degradation (ERAD). Our results clearly show that impaired secretion of the heterologous, hydrophobic CY028 cutinase in S. cerevisiae cells leads to protein aggregation in the ER, aberrant ER morphology and proliferation, and oxidative stress, as well as a UPR and ERAD.

scholarly journals Regulation of basal and induced levels of the MEL1 transcript in Saccharomyces cerevisiae.

1984 ◽  
Vol 4 (7) ◽  
pp. 1238-1245 ◽  
Author(s):  
M A Post-Beittenmiller ◽  
R W Hamilton ◽  
J E Hopper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Carbon Sources ◽  
Regulatory Proteins ◽  
Northern Hybridization ◽  
Transcriptional Expression ◽  
Wild Type ◽  
Naturally Occurring ◽  
Alpha Galactosidase ◽  
In Cells

The MEL1 gene in Saccharomyces cerevisiae is required for the production of alpha-galactosidase and for the catabolism of melibiose. Production of alpha-galactosidase is induced by galactose or melibiose and repressed by glucose. Inducibility is controlled by the positive and negative regulatory proteins GAL4 and GAL80, respectively. We have cloned the MEL1 gene to study its transcriptional expression and regulation. Evidence is presented that the MEL1 gene encodes alpha-galactosidase and that mel0 is a naturally occurring allele which lacks the alpha-galactosidase-coding sequences. RNAs prepared from wild-type cells and from cells carrying either the noninducible gal4-2 or GAL80S-100 allele grown on three different carbon sources were examined by Northern hybridization analyses. In wild-type cells under noninducing conditions, such as growth on glycerol-lactic acid, the MEL1 transcript was detected at a basal level which was 1 to 2% of the fully induced level. The basal level of expression was diminished in cells carrying the gal4-2 mutant allele but not in cells carrying the GAL80S-100 allele. The basal and induced RNA levels are repressed by glucose. Size determinations of the MEL1 transcripts detected in glycerol-lactic acid- and galactose-grown cells provided no evidence for two distinct transcripts.

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