Trehalose in yeast, stress protectant rather than reserve carbohydrate

Wiemken, Andres

doi:10.1007/bf00548935

Cited by 501 publications

(309 citation statements)

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“…Trehalose (α--glucopyranosyl α--glucopyranoside) is well known to act as a stress protectant in yeast and other organisms and displays potent protective effects against denaturation of proteins and other cellular components in itro [1,2]. In numerous studies a positive correlation has been observed between the trehalose level and stress resistance.…”

Section: Introductionmentioning

confidence: 99%

“…The function and the expression of the NTH2 Abbreviations used : PKA, cAMP-dependent protein kinase ; Nth1, neutral trehalase ; STRE, stress-responsive element. 1 To whom correspondence should be addressed (e-mail stefaan.wera!bio.kuleuven.ac.be). 2 Present address : Department of Biochemistry, University of Kentucky Medical Center, Lexington, KY 40536-0084, U.S.A.…”

Section: Introductionmentioning

confidence: 99%

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Opposite roles of trehalase activity in heat-shock recovery and heat-shock survival in Saccharomyces cerevisiae

Wera

Schrijver

Geyskens

et al. 1999

Biochemical Journal

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A variety of results has been obtained consistent with activation of neutral trehalase in Saccharomyces cerevisiae through direct phosphorylation by cAMP-dependent protein kinase (PKA). A series of neutral trehalase mutant alleles, in which all evolutionarily conserved putative phosphorylation sites were changed into alanine, was tested for activation in vitro (by PKA) and in vivo (by glucose addition). None of the mutations alone affected the activation ratio, whereas all mutations combined resulted in an inactive enzyme. All mutant alleles were expressed to similar levels, as shown by Western blotting. Several of the point mutations significantly lowered the specific activity. Using this series of mutants with different activity levels we show an inverse relationship between trehalase activity and heat-shock survival during glucose-induced trehalose mobilization. This is consistent with a stress-protective function of trehalose. On the other hand, reduction of trehalase activity below a certain threshold level impaired recovery from a sublethal heat shock. This suggests that trehalose breakdown is required for efficient recovery from heat shock, and that the presence of trehalase protein alone is not sufficient for efficient heat-stress recovery.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Opposite roles of trehalase activity in heat-shock recovery and heat-shock survival in Saccharomyces cerevisiae

Wera

Schrijver

Geyskens

et al. 1999

Biochemical Journal

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“…Interestingly, trehalose synthesis is induced in most of these organisms in response to a small set of specific environmental conditions. In particular, trehalose is accumulated in phases of nutrient starvation, desiccation, and after exposure to a mild heat shock (for reviews see Van Laere, 1989;Wiemken, 1990;Crowe et al, 1992). It has been suggested, therefore, that trehalose plays a role as a stabiliser of cellular structures under stress conditions (Keller et al, 1982;Crowe et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Structural analysis of the subunits of the trehalose‐6‐phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock

Reinders

Bürckert

Hohmann

et al. 1997

Molecular Microbiology

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SummarySynthesis of trehalose in the yeast Saccharomyces cerevisiae is catalysed by the trehalose-6-phosphate (Tre6P) synthase/phosphatase complex, which is composed of at least three different subunits encoded by the genes TPS1, TPS2, and TSL1. Previous studies indicated that Tps1 and Tps2 carry the catalytic activities of trehalose synthesis, namely Tre6P synthase (Tps1) and Tre6P phosphatase (Tps2), while Tsl1 was suggested to have regulatory functions. In this study two different approaches have been used to clarify the molecular composition of the trehalose synthase complex as well as the functional role of its potential subunits. Two-hybrid analyses of the in vivo interactions of Tps1, Tps2, Tsl1, and Tps3, a protein with high homology to Tsl1, revealed that both Tsl1 and Tps3 can interact with Tps1 and Tps2; the latter two proteins also interact with each other. In addition, trehalose metabolism upon heat shock was analysed in a set of 16 isogenic yeast strains carrying deletions of TPS1, TPS2, TSL1, and TPS3 in all possible combinations. These results not only confirm the previously suggested roles for Tps1 and Tps2, but also provide, for the first time, evidence that Tsl1 and Tps3 may share a common function with respect to regulation and/or structural stabilization of the Tre6P synthase/ phosphatase complex in exponentially growing, heatshocked cells.

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“…The accumulation of trehalost correlates with an mcredqe m thcrmotolcrance [ 1 I], suggesting that trehalosc IS a protective substance m yeast [12,13]. Enzyme measurements in extracts prepared by disruption of cells with glass beads at 4'C hdve C~~rrcr/~c,trkrlre urlrircrr A Wlcmkcn, Botatu~chc~ Instltul, Hcbclstrassc I, CH-405G Uascl, SwltzcrLmd fax (41) (61) 261 5318 yielded the surprising result that not only trehalose-Gphosphate synthase but also neutral trehalase actlvlty rapldly Increases upon heat shock, suggesting a high turn-over of trehalose during the heat shock [9] Considering the potential problems of the sampling procedure [8] mentioned above, we decided to reinvestigate the regulation of neutral trehalase under heat shock condltlons Here we report that the previously used extraction method [9] leads to artlficlally high actlvmes under heat shock condltlons apparently due to rapid phosphorylation during sampling.…”

Section: Introductionmentioning

confidence: 99%

A method to study the rapid phosphorylation‐related modulation of neutral trehalase activity by temperature shifts in yeast

et al. 1991

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I-Ieat shock enhanced the synthesis of neutral trehalase m growing cells of Saccl~a~omyce~ cerevrsrae, as detected by rmmunologlcal methods The actlvlty of the enzyme was measured m extracts obtamed by two methods cells were either harvested by filtration and subsequent dlsruptxon with glass beads at 0-4'C or Immediately frozen with hquld mtrogen m the presence of Trnton X-100, followed by thawmg at 30°C The first procedure yleldcd artlficlally high actlvltles of neutral trchalase m heat-shocked cells due to rapld (clmm) actlvatlon durmg handhng at 4°C before homogemzatlon Actlvlty of the enzyme m these homogenates decreased 75-90% upon a treatment with alkahne phosphatase, mdlcatmg that actlvatlon was due to phosphorylatlonThe second procedure ylelded low trehalase actlvltles for heat-shock treated cells, much higher actlvltles for cells shifted back for some seconds to 27'C, and very low actlvltles agam for cells shlfted from 27 to 40°C for a second tnne Thus. permeablhzatlon of cells followmg raprd frcezmg m Trlton X-100 IS a method of choice to study post-translational modulation of the neutral trehalase of S ccrcs~srae by phosphorylatlon and dcphosphorylahonTrehalase, Heat shock, Protem phosphorylatlon, Trehalose, S~cclraronry~e~ cerevrww

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Trehalose in yeast, stress protectant rather than reserve carbohydrate

Cited by 501 publications

References 38 publications

Opposite roles of trehalase activity in heat-shock recovery and heat-shock survival in Saccharomyces cerevisiae

Opposite roles of trehalase activity in heat-shock recovery and heat-shock survival in Saccharomyces cerevisiae

Structural analysis of the subunits of the trehalose‐6‐phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock

A method to study the rapid phosphorylation‐related modulation of neutral trehalase activity by temperature shifts in yeast

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