title: Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function.
abstract: Yeasts and filamentous fungi are endowed with two different trehalose-hydrolysing activities, termed acid and neutral trehalases according to their optimal pH for enzymatic activity. A wealth of information already exists on fungal neutral trehalases, while data on localization, regulation and function of fungal acid trehalases have remained elusive. The gene encoding the latter enzyme has now been isolated from two yeast species and two filamentous fungi, and sequences encoding putative acid trehalase can be retrieved from available public sequences. Despite weak similarities between amino acids sequences, this type of trehalase potentially harbours either a transmembrane segment or a signal peptide at the N-terminal sequence, as deduced from domain prediction algorithms. This feature, together with the demonstration that acid trehalase from yeasts and filamentous fungi is localized at the cell surface, is consistent with its main role in the utilisation of exogenous trehalose as a carbon source. The growth on this disaccharide is in fact pretty effective in most fungi except in Saccharomyces cerevisiae. This yeast species actually exhibits a "Kluyver effect" on trehalose. Moreover, an oscillatory behaviour reminiscent of what is observed in aerobic glucose-limited continuous cultures at low dilution rate is also observed in batch growth on trehalose. Finally, the S. cerevisiae acid trehalase may also participate in the catabolism of endogenous trehalose by a mechanism that likely requires the export of the disaccharide, its extracellular hydrolysis, and the subsequent uptake of the glucose released. Based on these recent findings, we suggest to rename "acid" and "neutral" trehalases as "extracellular" and "cytosolic" trehalases, which is more adequate to describe their localization and function in the fungal cell.
authors.affiliation: Centre de Bioingenierie Gilbert Durand, UMR-CNRS 5504, UMR-INRA 792, Institut National des Sciences Appliquées, 135 Avenue de Rangeuil, 31077 Toulouse cedex 04, France.
authors.forename: Jean Luc
authors.initials: JL
authors.lastname: Parrou
authors.forename: Matthieu
authors.initials: M
authors.lastname: Jules
authors.forename: Gemma
authors.initials: G
authors.lastname: Beltran
authors.forename: Jean
authors.initials: J
authors.lastname: François
mesh_terms: D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D005658:Fungi / Q000201:enzymology* / Q000235:genetics; D015966:Gene Expression Regulation, Fungal; D006863:Hydrogen-Ion Concentration; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D014198:Trehalase / Q000235:genetics / Q000378:metabolism*; D014199:Trehalose / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D014199:Trehalose; D014198:Trehalase