Deletion of the <i>ATH1</i> gene in <i>Saccharomyces cerevisiae</i> prevents growth on trehalose

Nwaka, Solomon; Mechler, Bernd; Holzer, Helmut

doi:10.1016/0014-5793(96)00450-4

Cited by 92 publications

(101 citation statements)

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“…In the sensitivity assay, cells are also allowed to grow to stationary phase, but 2 h prior to the heat shock they are diluted in fresh glucose-containing medium, and this treatment will initiate trehalose breakdown, at least in strains that contain active Nth1. As shown in Figure 4, nth1-deletion cells perform worse than the cells expressing wild-type trehalase in the recovery assay, confirming the poor heat-shockrecovery phenotype described previously for this mutant [4,5].…”

Section: Trehalase Activity Correlates With Heat-shock Sensitivity Ansupporting

confidence: 86%

“…Experimental evidence points to a role of trehalase in recovery from heat shock, and a nth1∆ strain displays a poor heat-shockrecovery phenotype [4,5]. Both mRNA levels and enzymic activity of Nth1 are increased upon mild heat stress.…”

Section: Trehalase Activity Correlates With Heat-shock Sensitivity Anmentioning

confidence: 99%

“…Remarkably, the NTH1-encoded neutral trehalase, which is responsible for trehalose breakdown, is also induced during sublethal heat treatment [4,5]. Since the nth1∆ mutant is impaired in recovery from heat shock, it has been proposed that mobilization of trehalose is important for recovery after heat stress.…”

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: Trehalase Activity Correlates With Heat-shock Sensitivity Ansupporting

confidence: 86%

Section: Trehalase Activity Correlates With Heat-shock Sensitivity Anmentioning

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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“…The resulting treA1 allele lacks the region encoding amino acids 41-1027 of the TreA protein. Since ⌬ath1 strains of S. cerevisiae are unable to grow on trehalose as a carbon source (Nwaka et al, 1996), pyr þ transformants obtained after transformation of an A. nidulans pyrG89 strain (FGSC773) with Not I-digested pTRE12 were tested for growth on minimal trehalose medium (see the Experimental procedures). Of the 75 pyr þ transformants tested, four displayed a residual growth pattern on minimal trehalose medium, similar to that observed when the carbon source is omitted.…”

Section: Disruption Of the Trea Genementioning

confidence: 99%

Molecular characterization of the Aspergillus nidulans treA gene encoding an acid trehalase required for growth on trehalose

d’Enfert

Fontaine

1997

Molecular Microbiology

107

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SummaryAspergillus nidulans conidiospores contain high levels of the non-reducing disaccharide trehalose. We show that upon induction of conidiospore germination, the trehalose pool is rapidly degraded and a glycerol pool is transiently accumulated. A trehalase with an acidic pH optimum was purified from conidiospores. Characterization of the treA gene encoding this trehalase shows that it is homologous to Saccharomyces cerevisiae vacuolar acid trehalase, the product of the ATH1 gene, and to two related proteins of unknown function identified in Mycobacterium tuberculosis and Mycobacterium leprae. A. nidulans mutants that lack acid trehalase activity were constructed by gene replacement at the treA locus. Analysis of these mutants suggests that the treA gene product is localized in the conidiospore wall, is required for growth on trehalose as a carbon source, and is not involved in the mobilization of the intracellular pool of trehalose. Therefore, it is proposed that a cytoplasmic regulatory trehalase is controlling this latter process.

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“…Recently, however, Jules et al (2004) proposed that Ath1 is mainly distributed in the extracellular space. It is known that Nth1 is responsible for degrading intracellular trehalose and Ath1 for hydrolyzing extracellular trehalose (Nwaka et al, 1996). Yet it is not clear how Ath1 gets access to the extracellular substrate nor how this hydrolase transits to the vacuole, although the early secretory pathway has been shown to be involved (Harris and Cotter, 1988 , 2006).…”

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The Transmembrane Domain of Acid Trehalase Mediates Ubiquitin-independent Multivesicular Body Pathway Sorting

Huang

Reggiori

Klionsky

2007

MBoC

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Trehalose serves as a storage source of carbon and plays important roles under various stress conditions. For example, in many organisms trehalose has a critical function in preserving membrane structure and fluidity during dehydration/ rehydration. In the yeast Saccharomyces cerevisiae, trehalose accumulates in the cell when the nutrient supply is limited but is rapidly degraded when the supply of nutrients is renewed. Hydrolysis of trehalose in yeast depends on neutral trehalase and acid trehalase (Ath1). Ath1 resides and functions in the vacuole; however, it appears to catalyze the hydrolysis of extracellular trehalose. Little is known about the transport route of Ath1 to the vacuole or how it encounters its substrate. Here, through the use of various trafficking mutants we showed that this hydrolase reaches its final destination through the multivesicular body (MVB) pathway. In contrast to the vast majority of proteins sorted into this pathway, Ath1 does not require ubiquitination for proper localization. Mutagenesis analyses aimed at identifying the unknown targeting signal revealed that the transmembrane domain of Ath1 contains the information sufficient for its selective sequestration into MVB internal vesicles. INTRODUCTIONTrehalose, a nonreducing disaccharide in which two glucose molecules are connected in an ␣-1,1-glycosidic linkage, was first found in the ergot of rye in 1832 (Kopp et al., 1993). This sugar is widely distributed in various organisms, including bacteria, fungi, plants, insects, and invertebrates (Elbein, 1974). It was originally believed that trehalose served only as a sugar and energy reserve in the cell; however, it is now known that this molecule also functions as a structural component, plays a role in transport, and is involved in signaling (Elbein et al., 2003). But the most significant function of trehalose is in providing membrane protection against different kinds of stress conditions, such as heat, freezing, dehydration, anoxia, and nutrient limitation (Crowe et al., 1984).Trehalose is quite common in yeast. In Saccharomyces cerevisiae, trehalose may constitute as much as 15-20% of its dry weight when growing in a stress environment. A strong correlation has been shown between trehalose content and stress resistance (Van Dijck et al., 1995). When yeast cells grow on rich carbon sources, they have a very low level of trehalose. In contrast, as they enter the stationary phase when nutrients are exhausted or during growth on nonfermentable carbon sources, the level of this disaccharide substantially increases. Conversely, when nutrients are resupplied, trehalose is rapidly mobilized (Nwaka and Holzer, 1998). The enzymes involved in synthesis and degradation of trehalose are the key regulators of these processes.Currently the best studied pathway of trehalose biosynthesis is the one that catalyzes UDP-glucose and glucose-6-phosphate into trehalose by trehalose-6-phosphate synthase and trehalose-phosphate-phosphatase activities (Thevelein, 1984). On the other hand, the degradation...

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Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose

Cited by 92 publications

References 34 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

Molecular characterization of the Aspergillus nidulans treA gene encoding an acid trehalase required for growth on trehalose

The Transmembrane Domain of Acid Trehalase Mediates Ubiquitin-independent Multivesicular Body Pathway Sorting

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