Response of D. hansenii to osmotic stress
Ontology highlight
ABSTRACT:
ORGANISM(S): Debaryomyces hansenii
PROVIDER: GSE9911 | GEO | 2008/03/15
SECONDARY ACCESSION(S): PRJNA103901
REPOSITORIES: GEO
Similar Datasets
Project description:Microarray analysis was used to identify the osmotic stress-responsive genes dependent on HogA and AtfA in the filamentous fungus Aspergillus nidulans. In order to identify such genes, we conducted the several types of experiment. One was a comparison between wild type with and without osmotic shock (Exp.6). Others were comparison between wild type with osmotic shock and each mutant (hogA, Exp.7; atfA, Exp.8) with osmotic shock. Compared the result of Exp.6 with other experiments, we could identify the genes whose expression was induced or repressed in response to osmotic stress in a manner dependent on HogA and AtfA. KEY WORD; Aspergillus nidulans, osmotic stress, HogA, AtfA
2009-06-16 | GSE16566 | GEO
Project description:Petelenz-kurdzeil2013 - Osmo adaptation
gpd1D
This model is described in the article:
Quantitative analysis of
glycerol accumulation, glycolysis and growth under hyper
osmotic stress.
Petelenz-Kurdziel E, Kuehn C,
Nordlander B, Klein D, Hong KK, Jacobson T, Dahl P, Schaber J,
Nielsen J, Hohmann S, Klipp E.
PLoS Comput. Biol. 2013; 9(6):
e1003084
Abstract:
We provide an integrated dynamic view on a eukaryotic
osmolyte system, linking signaling with regulation of gene
expression, metabolic control and growth. Adaptation to osmotic
changes enables cells to adjust cellular activity and turgor
pressure to an altered environment. The yeast Saccharomyces
cerevisiae adapts to hyperosmotic stress by activating the HOG
signaling cascade, which controls glycerol accumulation. The
Hog1 kinase stimulates transcription of genes encoding enzymes
required for glycerol production (Gpd1, Gpp2) and glycerol
import (Stl1) and activates a regulatory enzyme in glycolysis
(Pfk26/27). In addition, glycerol outflow is prevented by
closure of the Fps1 glycerol facilitator. In order to better
understand the contributions to glycerol accumulation of these
different mechanisms and how redox and energy metabolism as
well as biomass production are maintained under such conditions
we collected an extensive dataset. Over a period of 180 min
after hyperosmotic shock we monitored in wild type and
different mutant cells the concentrations of key metabolites
and proteins relevant for osmoadaptation. The dataset was used
to parameterize an ODE model that reproduces the generated data
very well. A detailed computational analysis using
time-dependent response coefficients showed that Pfk26/27
contributes to rerouting glycolytic flux towards lower
glycolysis. The transient growth arrest following hyperosmotic
shock further adds to redirecting almost all glycolytic flux
from biomass towards glycerol production. Osmoadaptation is
robust to loss of individual adaptation pathways because of the
existence and upregulation of alternative routes of glycerol
accumulation. For instance, the Stl1 glycerol importer
contributes to glycerol accumulation in a mutant with
diminished glycerol production capacity. In addition, our
observations suggest a role for trehalose accumulation in
osmoadaptation and that Hog1 probably directly contributes to
the regulation of the Fps1 glycerol facilitator. Taken
together, we elucidated how different metabolic adaptation
mechanisms cooperate and provide hypotheses for further
experimental studies.
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2024-09-02 | BIOMD0000000610 | BioModels
Project description:Dunaliella salina, a unicellular and eukaryotic alga, has been found as one of the most salt-tolerant eukaryote with a short growth period and wide practical applications. To elucidate the underlying molecular mechanism involved in the response to salinity and its different effects, RNA-seq was used for global transcriptome profiling of D. salina exposed to NaCl, Sorbiol and H2O2 stress. To maintain osmotic pressure homeostasis under suboptimal environment condition, starch breakdown catalyzed by both alpha-amylase (AMY) and glycogen phosphorylase (PYG) with consecutive expression patterns and low activity of PYG at the beginning of salt stress might be caused by a shortage of ATP because of impaired photosynthesis. Moreover, clustering analysis of differentially expressed genes (DEGs) indicated that starch and sucrose metabolism as well as glycerol metabolism reprogrammed under high salt stress only. For redox homeostasis, glycerol-3-phosphate shuttle performed by mitochondrial glycerol-3-phosphate dehydrogenases (GPDHs) participates the redox imbalance under abiotic stresses. c23777_g1 is a gene of D. salina involved in glycerol 3 phosphate (G3P) shuttle under various abiotic stresses while c25199_g1 is a gene of G3P shuttle induced only by osmotic stress.
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Project description:Jörg Schaber & Edda Klipp. Short-term volume and turgor regulation in yeast. Essays in Biochemistry 45 (2008).
We provide an integrated dynamic view on a eukaryotic osmolyte system, linking signaling with regulation of gene expression, metabolic control and growth. Adaptation to osmotic changes enables cells to adjust cellular activity and turgor pressure to an altered environment. The yeast Saccharomyces cerevisiae adapts to hyperosmotic stress by activating the HOG signaling cascade, which controls glycerol accumulation. The Hog1 kinase stimulates transcription of genes encoding enzymes required for glycerol production (Gpd1, Gpp2) and glycerol import (Stl1) and activates a regulatory enzyme in glycolysis (Pfk26/27). In addition, glycerol outflow is prevented by closure of the Fps1 glycerol facilitator. In order to better understand the contributions to glycerol accumulation of these different mechanisms and how redox and energy metabolism as well as biomass production are maintained under such conditions we collected an extensive dataset. Over a period of 180 min after hyperosmotic shock we monitored in wild type and different mutant cells the concentrations of key metabolites and proteins relevant for osmoadaptation. The dataset was used to parameterize an ODE model that reproduces the generated data very well. A detailed computational analysis using time-dependent response coefficients showed that Pfk26/27 contributes to rerouting glycolytic flux towards lower glycolysis. The transient growth arrest following hyperosmotic shock further adds to redirecting almost all glycolytic flux from biomass towards glycerol production. Osmoadaptation is robust to loss of individual adaptation pathways because of the existence and upregulation of alternative routes of glycerol accumulation. For instance, the Stl1 glycerol importer contributes to glycerol accumulation in a mutant with diminished glycerol production capacity. In addition, our observations suggest a role for trehalose accumulation in osmoadaptation and that Hog1 probably directly contributes to the regulation of the Fps1 glycerol facilitator. Taken together, we elucidated how different metabolic adaptation mechanisms cooperate and provide hypotheses for further experimental studies.
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Project description:Jörg Schaber & Edda Klipp. Short-term volume and turgor regulation in yeast. Essays in Biochemistry 45 (2008).
We provide an integrated dynamic view on a eukaryotic osmolyte system, linking signaling with regulation of gene expression, metabolic control and growth. Adaptation to osmotic changes enables cells to adjust cellular activity and turgor pressure to an altered environment. The yeast Saccharomyces cerevisiae adapts to hyperosmotic stress by activating the HOG signaling cascade, which controls glycerol accumulation. The Hog1 kinase stimulates transcription of genes encoding enzymes required for glycerol production (Gpd1, Gpp2) and glycerol import (Stl1) and activates a regulatory enzyme in glycolysis (Pfk26/27). In addition, glycerol outflow is prevented by closure of the Fps1 glycerol facilitator. In order to better understand the contributions to glycerol accumulation of these different mechanisms and how redox and energy metabolism as well as biomass production are maintained under such conditions we collected an extensive dataset. Over a period of 180 min after hyperosmotic shock we monitored in wild type and different mutant cells the concentrations of key metabolites and proteins relevant for osmoadaptation. The dataset was used to parameterize an ODE model that reproduces the generated data very well. A detailed computational analysis using time-dependent response coefficients showed that Pfk26/27 contributes to rerouting glycolytic flux towards lower glycolysis. The transient growth arrest following hyperosmotic shock further adds to redirecting almost all glycolytic flux from biomass towards glycerol production. Osmoadaptation is robust to loss of individual adaptation pathways because of the existence and upregulation of alternative routes of glycerol accumulation. For instance, the Stl1 glycerol importer contributes to glycerol accumulation in a mutant with diminished glycerol production capacity. In addition, our observations suggest a role for trehalose accumulation in osmoadaptation and that Hog1 probably directly contributes to the regulation of the Fps1 glycerol facilitator. Taken together, we elucidated how different metabolic adaptation mechanisms cooperate and provide hypotheses for further experimental studies.
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Project description:Jörg Schaber & Edda Klipp. Short-term volume and turgor regulation in yeast. Essays in Biochemistry 45 (2008).
We provide an integrated dynamic view on a eukaryotic osmolyte system, linking signaling with regulation of gene expression, metabolic control and growth. Adaptation to osmotic changes enables cells to adjust cellular activity and turgor pressure to an altered environment. The yeast Saccharomyces cerevisiae adapts to hyperosmotic stress by activating the HOG signaling cascade, which controls glycerol accumulation. The Hog1 kinase stimulates transcription of genes encoding enzymes required for glycerol production (Gpd1, Gpp2) and glycerol import (Stl1) and activates a regulatory enzyme in glycolysis (Pfk26/27). In addition, glycerol outflow is prevented by closure of the Fps1 glycerol facilitator. In order to better understand the contributions to glycerol accumulation of these different mechanisms and how redox and energy metabolism as well as biomass production are maintained under such conditions we collected an extensive dataset. Over a period of 180 min after hyperosmotic shock we monitored in wild type and different mutant cells the concentrations of key metabolites and proteins relevant for osmoadaptation. The dataset was used to parameterize an ODE model that reproduces the generated data very well. A detailed computational analysis using time-dependent response coefficients showed that Pfk26/27 contributes to rerouting glycolytic flux towards lower glycolysis. The transient growth arrest following hyperosmotic shock further adds to redirecting almost all glycolytic flux from biomass towards glycerol production. Osmoadaptation is robust to loss of individual adaptation pathways because of the existence and upregulation of alternative routes of glycerol accumulation. For instance, the Stl1 glycerol importer contributes to glycerol accumulation in a mutant with diminished glycerol production capacity. In addition, our observations suggest a role for trehalose accumulation in osmoadaptation and that Hog1 probably directly contributes to the regulation of the Fps1 glycerol facilitator. Taken together, we elucidated how different metabolic adaptation mechanisms cooperate and provide hypotheses for further experimental studies.
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Project description:Jörg Schaber & Edda Klipp. Short-term volume and turgor regulation in yeast. Essays in Biochemistry 45 (2008).
We provide an integrated dynamic view on a eukaryotic osmolyte system, linking signaling with regulation of gene expression, metabolic control and growth. Adaptation to osmotic changes enables cells to adjust cellular activity and turgor pressure to an altered environment. The yeast Saccharomyces cerevisiae adapts to hyperosmotic stress by activating the HOG signaling cascade, which controls glycerol accumulation. The Hog1 kinase stimulates transcription of genes encoding enzymes required for glycerol production (Gpd1, Gpp2) and glycerol import (Stl1) and activates a regulatory enzyme in glycolysis (Pfk26/27). In addition, glycerol outflow is prevented by closure of the Fps1 glycerol facilitator. In order to better understand the contributions to glycerol accumulation of these different mechanisms and how redox and energy metabolism as well as biomass production are maintained under such conditions we collected an extensive dataset. Over a period of 180 min after hyperosmotic shock we monitored in wild type and different mutant cells the concentrations of key metabolites and proteins relevant for osmoadaptation. The dataset was used to parameterize an ODE model that reproduces the generated data very well. A detailed computational analysis using time-dependent response coefficients showed that Pfk26/27 contributes to rerouting glycolytic flux towards lower glycolysis. The transient growth arrest following hyperosmotic shock further adds to redirecting almost all glycolytic flux from biomass towards glycerol production. Osmoadaptation is robust to loss of individual adaptation pathways because of the existence and upregulation of alternative routes of glycerol accumulation. For instance, the Stl1 glycerol importer contributes to glycerol accumulation in a mutant with diminished glycerol production capacity. In addition, our observations suggest a role for trehalose accumulation in osmoadaptation and that Hog1 probably directly contributes to the regulation of the Fps1 glycerol facilitator. Taken together, we elucidated how different metabolic adaptation mechanisms cooperate and provide hypotheses for further experimental studies.
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Project description:Jörg Schaber & Edda Klipp. Short-term volume and turgor regulation in yeast. Essays in Biochemistry 45 (2008).
We provide an integrated dynamic view on a eukaryotic osmolyte system, linking signaling with regulation of gene expression, metabolic control and growth. Adaptation to osmotic changes enables cells to adjust cellular activity and turgor pressure to an altered environment. The yeast Saccharomyces cerevisiae adapts to hyperosmotic stress by activating the HOG signaling cascade, which controls glycerol accumulation. The Hog1 kinase stimulates transcription of genes encoding enzymes required for glycerol production (Gpd1, Gpp2) and glycerol import (Stl1) and activates a regulatory enzyme in glycolysis (Pfk26/27). In addition, glycerol outflow is prevented by closure of the Fps1 glycerol facilitator. In order to better understand the contributions to glycerol accumulation of these different mechanisms and how redox and energy metabolism as well as biomass production are maintained under such conditions we collected an extensive dataset. Over a period of 180 min after hyperosmotic shock we monitored in wild type and different mutant cells the concentrations of key metabolites and proteins relevant for osmoadaptation. The dataset was used to parameterize an ODE model that reproduces the generated data very well. A detailed computational analysis using time-dependent response coefficients showed that Pfk26/27 contributes to rerouting glycolytic flux towards lower glycolysis. The transient growth arrest following hyperosmotic shock further adds to redirecting almost all glycolytic flux from biomass towards glycerol production. Osmoadaptation is robust to loss of individual adaptation pathways because of the existence and upregulation of alternative routes of glycerol accumulation. For instance, the Stl1 glycerol importer contributes to glycerol accumulation in a mutant with diminished glycerol production capacity. In addition, our observations suggest a role for trehalose accumulation in osmoadaptation and that Hog1 probably directly contributes to the regulation of the Fps1 glycerol facilitator. Taken together, we elucidated how different metabolic adaptation mechanisms cooperate and provide hypotheses for further experimental studies.
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