Literature DB >> 8647289

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

S Nwaka1, B Mechler, H Holzer.   

Abstract

The biological function of the yeast trehalases (EC 3.2.1.28) consists of down-regulation of the concentration of trehalose via glucose formation by trehalose hydrolysis. While it is generally accepted that the cytosolic neutral trehalase (encoded by the NTH1 gene) is responsible for trehalose hydrolysis in intact cells, very little is known about a role of the vacuolar acid trehalase and the product of the recently described neutral trehalase gene YBRO106 (NTH2). We have analyzed the role of the acid trehalase in trehalose hydrolysis using the ATH1 deletion mutant (delta ath1) of Saccharomyces cerevisiae [M. Destruelle et al. (1995) Yeast 11, 1015-10251 deficient in acid trehalase activity under various nutritional conditions. In contrast to wild-type and a mutant deficient in the neutral trehalase (delta nth1), the delta ath1 mutant does not grow on trehalose as a carbon source. Experiments with diploid strains heterozygous for delta ath1 show a gene dosage effect for the ATH1 gene for growth on trehalose. The need for acid trehalase for growth on trehalose is supported by the finding that acid trehalase activity is induced during exponential growth of cells on trehalose while no such induction is measurable during growth on glucose. Our results show that the vacuolar acid trehalase Ath1p is necessary for the phenotype of growth on trehalose, i.e. trehalose utilization, in contrast to cytosolic neutral trehalase Nth1p which is necessary for intracellular degradation of trehalose. For explanation of the need for vacuolar acid trehalase and not cytosolic neutral trehalase for growth on trehalose, the participation of endocytosis for uptake of trehalose from medium to the vacuoles is discussed.

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Year:  1996        PMID: 8647289     DOI: 10.1016/0014-5793(96)00450-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  21 in total

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

Authors:  S Wera; E De Schrijver; I Geyskens; S Nwaka; J M Thevelein
Journal:  Biochem J       Date:  1999-11-01       Impact factor: 3.857

2.  Stress tolerance in doughs of Saccharomyces cerevisiae trehalase mutants derived from commercial Baker's yeast.

Authors:  J Shima; A Hino; C Yamada-Iyo; Y Suzuki; R Nakajima; H Watanabe; K Mori; H Takano
Journal:  Appl Environ Microbiol       Date:  1999-07       Impact factor: 4.792

3.  Elevated growth of Saccharomyces cerevisiae ATH1 null mutants on glucose is an artifact of nonmatching auxotrophies of mutant and reference strains.

Authors:  R Chopra; V M Sharma; K Ganesan
Journal:  Appl Environ Microbiol       Date:  1999-05       Impact factor: 4.792

4.  Accumulation of trehalose by overexpression of tps1, coding for trehalose-6-phosphate synthase, causes increased resistance to multiple stresses in the fission yeast schizosaccharomyces pombe

Authors: 
Journal:  Appl Environ Microbiol       Date:  1999-05       Impact factor: 4.792

5.  Trehalose and trehalase in Arabidopsis.

Authors:  J Müller; R A Aeschbacher; A Wingler; T Boller; A Wiemken
Journal:  Plant Physiol       Date:  2001-02       Impact factor: 8.340

6.  Enhanced freeze tolerance of baker's yeast by overexpressed trehalose-6-phosphate synthase gene (TPS1) and deleted trehalase genes in frozen dough.

Authors:  Haigang Tan; Jian Dong; Guanglu Wang; Haiyan Xu; Cuiying Zhang; Dongguang Xiao
Journal:  J Ind Microbiol Biotechnol       Date:  2014-06-21       Impact factor: 3.346

7.  Role of nitrogen and carbon transport, regulation, and metabolism genes for Saccharomyces cerevisiae survival in vivo.

Authors:  Joanne M Kingsbury; Alan L Goldstein; John H McCusker
Journal:  Eukaryot Cell       Date:  2006-05

Review 8.  Vacuolar hydrolysis and efflux: current knowledge and unanswered questions.

Authors:  Katherine R Parzych; Daniel J Klionsky
Journal:  Autophagy       Date:  2018-11-22       Impact factor: 16.016

9.  The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting.

Authors:  Ju Huang; Fulvio Reggiori; Daniel J Klionsky
Journal:  Mol Biol Cell       Date:  2007-05-02       Impact factor: 4.138

10.  Trehalose-enzyme interactions result in structure stabilization and activity inhibition. The role of viscosity.

Authors:  José G Sampedro; Salvador Uribe
Journal:  Mol Cell Biochem       Date:  2004 Jan-Feb       Impact factor: 3.396

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