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Applied and Environmental Microbiology, February 2008, p. 605-614, Vol. 74, No. 3
0099-2240/08/$08.00+0     doi:10.1128/AEM.00557-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

New Insights into Trehalose Metabolism by Saccharomyces cerevisiae: NTH2 Encodes a Functional Cytosolic Trehalase, and Deletion of TPS1 Reveals Ath1p-Dependent Trehalose Mobilization{triangledown} ,{dagger}

Matthieu Jules,{ddagger},§ Gemma Beltran,{ddagger},¶ Jean François,* and Jean Luc Parrou

UMR 5504 & UMR 792 d'Ingénierie des Systèmes Biologiques et des Procédés, CNRS-INRA-INSA, F-31077 Toulouse, France

Received 10 March 2007/ Accepted 20 November 2007

In the yeast Saccharomyces cerevisiae, the synthesis of endogenous trehalose is catalyzed by a trehalose synthase complex, TPS, and its hydrolysis relies on a cytosolic/neutral trehalase encoded by NTH1. In this work, we showed that NTH2, a paralog of NTH1, encodes a functional trehalase that is implicated in trehalose mobilization. Yeast is also endowed with an acid trehalase encoded by ATH1 and an H+/trehalose transporter encoded by AGT1, which can together sustain assimilation of exogenous trehalose. We showed that a tps1 mutant defective in the TPS catalytic subunit cultivated on trehalose, or on a dual source of carbon made of galactose and trehalose, accumulated high levels of intracellular trehalose by its Agt1p-mediated transport. The accumulated disaccharide was mobilized as soon as cells entered the stationary phase by a process requiring a coupling between its export and immediate extracellular hydrolysis by Ath1p. Compared to what is seen for classical growth conditions on glucose, this mobilization was rather unique, since it took place prior to that of glycogen, which was postponed until the late stationary phase. However, when the Ath1p-dependent mobilization of trehalose identified in this study was impaired, glycogen was mobilized earlier and faster, indicating a fine-tuning control in carbon storage management during periods of carbon and energy restriction.

* Corresponding author. Mailing address: UMR 5504 & UMR 792 d'Ingénierie des Systèmes Biologiques et des Procédés, Institut national des Sciences Appliquées, 135 Avenue de Rangueil, 31077 Toulouse cedex 04, France. Phone: 33 5 61 559492. Fax: 33 5 61 559400. E-mail: fran_jm{at}insa-toulouse.fr

{triangledown} Published ahead of print on 7 December 2007.

{dagger} This paper is dedicated to Carlos and Juana Maria Gancedo, friends and colleagues, for their outstanding contributions to the field of yeast biochemistry.

{ddagger} These two authors contributed equally to this work.

§ Present address: Unit Genomics of Microbial Pathogens, Institut Pasteur, Paris, France.

Present address: Department of Cellular and Molecular Biology, Goeteborg, Sweden.

Applied and Environmental Microbiology, February 2008, p. 605-614, Vol. 74, No. 3
0099-2240/08/$08.00+0     doi:10.1128/AEM.00557-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Pacheco, A., Pereira, C., Almeida, M. J., Sousa, M. J. (2009). Small heat-shock protein Hsp12 contributes to yeast tolerance to freezing stress. Microbiology 155: 2021-2028 [Abstract] [Full Text]  


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