New Insights into Trehalose Metabolism by Saccharomyces cerevisiae: NTH2 Encodes a Functional Cytosolic Trehalase, and Deletion of TPS1 Reveals Ath1p-Dependent Trehalose Mobilization▿ †
| Autor: | Jules, Matthieu, Beltran, Gemma, François, Jean marie, Parrou, Jean-Luc |
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| Přispěvatelé: | Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), ACI program 'Microbiology and Pathogenicity' of the French Ministry of Education, G.B. was supported by a 1-year Marie Curie Young Training Fellowship (no. HPMT-EC-2000-00135) as part of her Ph.D. thesis, M.J. was supported by a doctoral grant from the French Ministry of Education and Research., Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
Saccharomyces cerevisiae Proteins Trehalose Saccharomyces cerevisiae acid trehalase Physiology and Biotechnology Yeast NTH1 NTH2 Culture Media Cytosol neutral trehalase Glucosyltransferases ATH1 [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] transport physiology Mutation TPS1 Trehalase [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology Glycogen |
| Zdroj: | Applied and Environmental Microbiology Applied and Environmental Microbiology, 2008, 74 (3), pp.605-614. ⟨10.1128/AEM.00557-07⟩ Applied and Environmental Microbiology, American Society for Microbiology, 2008, 74 (3), pp.605-614. ⟨10.1128/AEM.00557-07⟩ |
| ISSN: | 0099-2240 1098-5336 |
| Popis: | International audience; 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 |
| Databáze: | OpenAIRE |
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