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Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function.
FEMS Yeast Res 2005; 5(6-7):503-11FY

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+Show Affiliations

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.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

15780651

Citation

Parrou, Jean Luc, et al. "Acid Trehalase in Yeasts and Filamentous Fungi: Localization, Regulation and Physiological Function." FEMS Yeast Research, vol. 5, no. 6-7, 2005, pp. 503-11.
Parrou JL, Jules M, Beltran G, et al. Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function. FEMS Yeast Res. 2005;5(6-7):503-11.
Parrou, J. L., Jules, M., Beltran, G., & François, J. (2005). Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function. FEMS Yeast Research, 5(6-7), pp. 503-11.
Parrou JL, et al. Acid Trehalase in Yeasts and Filamentous Fungi: Localization, Regulation and Physiological Function. FEMS Yeast Res. 2005;5(6-7):503-11. PubMed PMID: 15780651.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Acid trehalase in yeasts and filamentous fungi: localization, regulation and physiological function. AU - Parrou,Jean Luc, AU - Jules,Matthieu, AU - Beltran,Gemma, AU - François,Jean, PY - 2004/08/26/received PY - 2004/12/15/revised PY - 2005/01/14/accepted PY - 2005/3/23/pubmed PY - 2005/6/10/medline PY - 2005/3/23/entrez SP - 503 EP - 11 JF - FEMS yeast research JO - FEMS Yeast Res. VL - 5 IS - 6-7 N2 - 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. SN - 1567-1356 UR - https://www.unboundmedicine.com/medline/citation/15780651/Acid_trehalase_in_yeasts_and_filamentous_fungi:_localization_regulation_and_physiological_function_ L2 - https://academic.oup.com/femsyr/article-lookup/doi/10.1016/j.femsyr.2005.01.002 DB - PRIME DP - Unbound Medicine ER -