Heat shock induces enzymes of trehalose metabolism, trehalose accumulation, and thermotolerance in <i>Schizosaccharomyces pombe</i>, even in the presence of cycloheximide

Virgilio, Claudio De; Simmen, Urs; Hottiger, Thomas; Boiler, Thomas; Wiemken, Andres

doi:10.1016/0014-5793(90)81062-s

Cited by 101 publications

(77 citation statements)

References 16 publications

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“…Gaps (-) were introduced to optimise alignment. mide in S. cerevisiae (Panek et a1.,1990), but apparently not in Schizosaccharomyces pombe (De Virgilio et al, 1990). Our results (Fig.…”

Section: Tsll Rirgihkkllayekflvenpeyvekstliq------icigsskdve----lerqisupporting

confidence: 40%

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Vuorio¹,

Kalkkinen

Londesborough³

1993

European Journal of Biochemistry

143

127

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Preparations of intact trehalose synthase contain three polypeptides with molecular masses of 56, 102 and 123 kDa. We have cloned the genes TSSl and TSLl coding for the 56-and 123-kDa subunits, respectively. These genes are located on chromosomes I1 (TSSI) and XI11 (TSLI). The TSSl gene was found to be identical with ClFl, a gene required for normal growth on glucose. The product of the entire TSSl gene exibits 37% identity with a 502-amino-acid stretch from the middle of the TSLl product. Disruption of the TSSl gene in yeast eliminates both trehalose 6-phosphate synthase (Tre6P synthase) and trehalose 6-phosphate phosphatase (Tre6Pase) activities, and reintroduction of this gene restores these activities. Transformation of Escherichia coli with TSSl increases its Tre6P synthase activity. Specific proteolytic degradation of the 123-kDa polypeptide from the N-terminus greatly influences the Tre6P synthase activity, decreasing its inhibition by phosphate and activatability by fructose 6-phosphate but has little effect on the Tre6Pase activity. These results suggest that this N-terminal part confers regulatory properties upon the Tre6P synthase activity.Trehalose, a non-reducing disaccharide of glucose, occurs in Saccharomyces cerevisiae during periods of reduced growth, such as during starvation of cells for nitrogen, phosphate or sulfur, as well as during the stationary phase after growth on glucose (Lillie and Pringle, 1980). It is also accumulated in cells exposed to extremes of temperature, dehydration or hazardous chemicals (Attfield, 1987 ;Hottiger et al., 1987;Hino et al., 1990). Experiments using mutants producing varying amounts of trehalose and the increases in intracellular trehalose concentration caused by heat-shock treatment, have shown that heat tolerance, as well as desiccation tolerance, are closely related to the trehalose content of the yeast cell (Hottiger et al., 1987).The formation of trehalose is catalysed by the sequential action of trehalose-6-phosphate synthase (Tre6P synthase) and trehalose-6-phosphate phosphatase (Tre6Pase) activities. These activities co-elute through several chromatographic procedures, suggesting that they are part of a single bifunctional protein (Vandercammen et al., 1989 ;Londesborough and Vuorio, 1991). A protein complex, called trehalose synthase, has been purified in a specifically proteolysed form (Londesborough and Vuorio, 1991) and an apparently intact form (Vuorio et al

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“…Gaps (-) were introduced to optimise alignment. mide in S. cerevisiae (Panek et a1.,1990), but apparently not in Schizosaccharomyces pombe (De Virgilio et al, 1990). Our results (Fig.…”

Section: Tsll Rirgihkkllayekflvenpeyvekstliq------icigsskdve----lerqisupporting

confidence: 40%

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Vuorio¹,

Kalkkinen

Londesborough³

1993

European Journal of Biochemistry

143

127

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“…However, that possibility seems less likely, as induction of thermotolerance in mRNA export requires new protein translation during mild heat pre-treatment (Tani et al, 1995) and also during mild saline pretreatment (data not shown). For the same reason, the involvement of trehalose, the accumulation of which does not require protein synthesis (De Virgilio et al, 1990), in mRNA export thermotolerance seems to be unlikely.…”

Section: Discussionmentioning

confidence: 99%

Hsp16p Is Required for Thermotolerance in Nuclear mRNA Export in Fission Yeast Schizosaccharomyces pombe

Yoshida

Tani

2005

Cell Struct. Funct.

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ABSTRACT. Export of mRNA from the nucleus to the cytoplasm is one of the essential steps for eukaryotic gene expression. In the fission yeast Schizosaccharomyces pombe, heat shock stress at 42°C causes block of mRNA export from the nucleus. We now report that saline and ethanol stresses also inhibit nuclear mRNA export, resulting in accumulation of bulk poly (A)+ RNA, as well as a specific mRNA, in the nucleus. Under stressed conditions, an mRNA export receptor Mex67p relocates to the nucleolus from the nuclear periphery and this relocation is closely correlated with inhibition of mRNA export by the stresses. Pretreatment of cells with a mild saline stress induced thermotolerance in mRNA export in a similar manner seen with mild heat pretreatment and protected mRNA export machinery from the subsequent severe heat shock. In contrast, mild ethanol stress could not induce the thermotolerance in mRNA export, suggesting that the stress response induced by ethanol differs from that induced by saline and heat shock stresses. In addition, we found that the Spc1p MAPK pathway is involved in induction of thermotolerance in mRNA export. Of the downstream targets for Spc1p, the Atf1p transcription factor was essential for induction of thermotolerance in mRNA export. We also found that Hsp16p, the expression of which is controlled by Atf1p, is involved in acquisition of thermotolerance in mRNA export in S. pombe.

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“…One factor potentially important for the development of induced thermotolerance in yeast, is the heat-induced accumulation of the non-reducing disaccharide trehalose (a-D-glucopyranosyl-1,l-a-D-glucopyranoside). In previous studies, we have shown that trehalose levels and thermotolerance are correlated under a variety of experimental conditions in both wild-type strains and regulatory mutants with altered pools of trehalose (Hottiger et al, 1987a(Hottiger et al, ,b, 1989De Virgilio et al, 1990, 1991aHottiger et al, 1992). Also, we have shown that trehalose accumulation and the acquisition of thermotolerance during heat shock are partially independent of protein synthesis in Saccharomyces cerevisiae (De Virgilio et al, 1991a) and completely independent of protein synthesis in Schizosaccharomyces pombe (De Virgilio et al, 1990).…”

mentioning

confidence: 84%

“…In previous studies, we have shown that trehalose levels and thermotolerance are correlated under a variety of experimental conditions in both wild-type strains and regulatory mutants with altered pools of trehalose (Hottiger et al, 1987a(Hottiger et al, ,b, 1989De Virgilio et al, 1990, 1991aHottiger et al, 1992). Also, we have shown that trehalose accumulation and the acquisition of thermotolerance during heat shock are partially independent of protein synthesis in Saccharomyces cerevisiae (De Virgilio et al, 1991a) and completely independent of protein synthesis in Schizosaccharomyces pombe (De Virgilio et al, 1990). Therefore, we suggested that trehalose, which was originally thought to function as a storage carbohydrate in yeast, may actually be a stress protectant involved in induced thermotolerance and other phenomena of stress protection (Wiemken, 1990).…”

mentioning

confidence: 99%

The role of trehalose synthesis for the acquisition of thermotolerance in yeast

Virgilio

Hottiger

Domínguez

et al. 1994

European Journal of Biochemistry

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300

201

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In the yeast Saccharomyces cerevisiae, accumulation of the non-reducing disaccharide trehalose is triggered by various stimuli that activate the heat-schock response. Several studies have shown a close correlation between trehalose levels and tolerance to heat stress, suggesting that trehalose may be a protectant which contributes to thermotolerance. In this study, we have examined mutants defective in genes coding for key enzymes involved in trehalose metabolism with respect to the heat-induced and stationary-phase-induced accumulation of trehalose and the acquisition of thermotolerance. Inactivation of either TPSl or TPS2, encoding subunits of the trehalose-6-phosphate synthase/phosphatase complex, caused an inability to accumulate trehalose upon a mild heat-shock or upon initiation of the stationary phase and significantly reduced the levels of heat-induced and stationary-phase-induced thermotolerance. Deletion of NTHZ, the gene coding for the neutral trehalase, resulted in a defect in trehalose mobilization during recovery from a heat shock which was paralleled by an abnormally slow decrease of thermotolerance. Our results provide strong genetic evidence that heat-induced synthesis of trehalose is an important factor for thermotolerance induction. In an accompanying study [Hottiger, T

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Heat shock induces enzymes of trehalose metabolism, trehalose accumulation, and thermotolerance in Schizosaccharomyces pombe, even in the presence of cycloheximide

Cited by 101 publications

References 16 publications

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Hsp16p Is Required for Thermotolerance in Nuclear mRNA Export in Fission Yeast Schizosaccharomyces pombe

The role of trehalose synthesis for the acquisition of thermotolerance in yeast

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