Trehalose-Mediated Inhibition of the Plasma Membrane H
            <sup>+</sup>
            -ATPase from
            <i>Kluyveromyces lactis</i>
            : Dependence on Viscosity and Temperature

Sampedro, José G.; Muñoz‐Clares, Rosario A.; Uribe, Salvador

doi:10.1128/jb.184.16.4384-4391.2002

Cited by 32 publications

(50 citation statements)

References 45 publications

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“…The rate constant for the ATPase reaction (V max = k cat [E t ]) was inversely dependent on solution viscosity; as higher the viscosity lower the reaction rate of catalysis (Sampedro et al, 2002). Notably, when temperature was raised inhibition disappeared, in agreement with the fact that viscosity decreases when temperature increases (Table 1).…”

Section: Inhibition Of Isolated Enzymes; Possible Role Of Viscositysupporting

confidence: 64%

“…The plasma membrane H + -ATPase from yeast depends on large domain motion for catalysis (Kulbrandt, 2004), was inhibited at all trehalose concentrations tested (Sampedro et al, 2002). The rate constant for the ATPase reaction (V max = k cat [E t ]) was inversely dependent on solution viscosity; as higher the viscosity lower the reaction rate of catalysis (Sampedro et al, 2002).…”

Section: Inhibition Of Isolated Enzymes; Possible Role Of Viscositymentioning

confidence: 99%

See 1 more Smart Citation

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Araiza‐Olivera¹,

Uribe‐Carvajal²,

Chiquete-Félix³

et al. 2012

Cell Metabolism - Cell Homeostasis and Stress Response

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Section: Inhibition Of Isolated Enzymes; Possible Role Of Viscositysupporting

confidence: 64%

Section: Inhibition Of Isolated Enzymes; Possible Role Of Viscositymentioning

confidence: 99%

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Araiza‐Olivera¹,

Uribe‐Carvajal²,

Chiquete-Félix³

et al. 2012

Cell Metabolism - Cell Homeostasis and Stress Response

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“…The data from Bubnik, Kadlec, Urban, and Bruhns (1995) (for sucrose solutions) and from Sampedro, Muñoz-Clares, and Uribe (2002) (for trehalose solutions) where also plotted in Fig. 1 for the purpose of comparison; it is to be noted that the data from Sampedro et al (2002) corresponds to a lower range of trehalose concentration following the same tendency as present data. Although data for viscosity of sucrose solutions are available from literature, they were also measured in order to check the reliability of our determinations.…”

Section: Comparison Of the Viscosity Of Trehalose And Sucrose Solutionsmentioning

confidence: 70%

Comparison of the viscosity of trehalose and sucrose solutions at various temperatures: Effect of guar gum addition

Galmarini

Baeza

Sánchez

et al. 2011

LWT - Food Science and Technology

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“…The transcription of NTH1 is stress responsive (62); however, the activity of Nth1 is greater during recovery from stress (39), allowing Nth1 to successfully compete with the biosynthetic pathway and reduce intracellular trehalose levels (28). This degradation of trehalose is critical for recovery from heat shock (59) as very high levels of trehalose can interfere with normal protein activity by stabilizing proteins in nonnative conformations and inhibiting the refolding of these denatured proteins by HSPs (12,43,44,46,56). Taken together, these data have led to a temporal model of trehalose function as a cochaperone during the heat shock response: trehalose functions to protect proteins at the initial stages of the heat shock response before HSPs have been fully induced, but trehalose must be degraded in order for the HSPs to fully assist the cell in recovery from heat shock (47).…”

mentioning

confidence: 99%

The Natural Osmolyte Trehalose Is a Positive Regulator of the Heat-Induced Activity of Yeast Heat Shock Transcription Factor

Conlin

Nelson

2007

Molecular and Cellular Biology

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In Saccharomyces cerevisiae, the intracellular concentration of trehalose increases rapidly in response to many environmental stresses, including heat shock. These high trehalose levels have been correlated with tolerance to adverse conditions and led to the model that trehalose functions as a chemical cochaperone. Here, we show that the transcriptional activity of Hsf1 during the heat shock response depends on trehalose. Strains with low levels of trehalose have a diminished transcriptional response to heat shock, while strains with high levels of trehalose have an enhanced transcriptional response to heat shock. The enhanced transcriptional response does not require the other heat-responsive transcription factors Msn2/4 but is dependent upon heat and Hsf1. In addition, the phosphorylation levels of Hsf1 correlate with both transcriptional activity and the presence of trehalose. These in vivo results support a new role for trehalose, where trehalose directly modifies the dynamic range of Hsf1 activity and therefore influences heat shock protein mRNA levels in response to stress.Trehalose is a disaccharide of glucose that is found predominantly in bacteria, fungi (including yeasts), plants, and invertebrates. This natural osmolyte was initially characterized as a storage carbohydrate due to the high intracellular concentrations observed during these organisms' resting and anhydrobiotic states (reviewed in reference 55). Since these states involve the ability to survive stressful conditions, trehalose levels were then linked to thermotolerance, the ability of an organism to survive an otherwise lethal heat shock (reviewed in reference 47). Trehalose has been shown to stabilize the structures and enzymatic activities of proteins against thermal denaturation in vitro (15,27,63). In addition, trehalose can prevent the aggregation of misfolded proteins, including amyloidogenic proteins (3,11,27,33,46,52), and is being considered for clinical trials for Huntington's disease (53). Trehalose is more effective than other sugars in protecting proteins against thermal denaturation and aggregation because of its unusual ability to alter the water environment surrounding a protein, stabilizing the protein in its native conformation (1,30,34,48).In the yeast Saccharomyces cerevisiae, trehalose levels vary depending on the environment of the cell. The levels are almost undetectable during normal exponential growth. After heat shock, trehalose levels increase rapidly and dramatically, along with the accumulation of heat shock proteins (HSPs) (26,28). This rapid increase in trehalose has been attributed to the increase in both the translation of the genes involved in the synthesis of trehalose (TPS1 and TPS2) (4, 41, 58) and the substrates required for trehalose synthesis (1, 61). In addition, the enzymatic activity of TPS1 increases during the heat shock response (1, 38). High trehalose levels can stabilize enzymatic activity and can prevent the aggregation of exogenous proteins in vivo during heat shock (45,46). Trehalose is d...

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Trehalose-Mediated Inhibition of the Plasma Membrane H ⁺ -ATPase from Kluyveromyces lactis : Dependence on Viscosity and Temperature

Cited by 32 publications

References 45 publications

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Comparison of the viscosity of trehalose and sucrose solutions at various temperatures: Effect of guar gum addition

The Natural Osmolyte Trehalose Is a Positive Regulator of the Heat-Induced Activity of Yeast Heat Shock Transcription Factor

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Trehalose-Mediated Inhibition of the Plasma Membrane H + -ATPase from Kluyveromyces lactis : Dependence on Viscosity and Temperature

Cited by 32 publications

References 45 publications

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Comparison of the viscosity of trehalose and sucrose solutions at various temperatures: Effect of guar gum addition

The Natural Osmolyte Trehalose Is a Positive Regulator of the Heat-Induced Activity of Yeast Heat Shock Transcription Factor

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About

Trehalose-Mediated Inhibition of the Plasma Membrane H ⁺ -ATPase from Kluyveromyces lactis : Dependence on Viscosity and Temperature