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Function and regulation of the acid and neutral trehalases of Mucor rouxii.
FEMS Microbiol Lett 1997; 155(1):73-7FM

Abstract

Two different trehalose-hydrolysing activities, known as acid or non-regulatory trehalases, and neutral or regulatory trehalases, have been recognised in a number of fungal species. The true role of these apparently redundant hydrolases remained obscure for many years. However, recent evidence suggests that neutral trehalases would be specialised in the mobilisation of cytosolic trehalose, while acid trehalases would only hydrolyse extracellular trehalose. Results obtained with Mucor rouxii, a Zygomycete initially thought to possess only neutral trehalase activity, reinforced this hypothesis. M. rouxii grows efficiently in trehalose as the sole carbon source. Trehalose-grown or carbon-starved cells exhibit a high trehalase activity of optimum pH 4.5, bound to the external surface of the cell wall, in contrast with the neutral (pH 6.5) trehalase, which occurs in the cytosol. Other differences between the neutral and the acid trehalases are the temperature optimum (35 degrees C and 45 degrees C, respectively) and thermal stability (half-life of 2.5 min and 12 min at 45 degrees C, respectively). The neutral trehalase, but not the acid trehalase, is activated in vitro by cAMP-dependent phosphorylation, stimulated by Ca2+, and inhibited by EDTA. It shows maximal activity at germination and decreases as growth proceeds. In contrast the activity of the acid trehalase is totally repressed in glucose-grown cultures and increases upon exhaustion of the carbon source, and is strongly induced by extracellular trehalose.

Authors+Show Affiliations

Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Brazil.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9345767

Citation

de Almeida, F M., et al. "Function and Regulation of the Acid and Neutral Trehalases of Mucor Rouxii." FEMS Microbiology Letters, vol. 155, no. 1, 1997, pp. 73-7.
de Almeida FM, Lúcio AK, Polizeli ML, et al. Function and regulation of the acid and neutral trehalases of Mucor rouxii. FEMS Microbiol Lett. 1997;155(1):73-7.
de Almeida, F. M., Lúcio, A. K., Polizeli, M. L., Jorge, J. A., & Terenzi, H. F. (1997). Function and regulation of the acid and neutral trehalases of Mucor rouxii. FEMS Microbiology Letters, 155(1), pp. 73-7.
de Almeida FM, et al. Function and Regulation of the Acid and Neutral Trehalases of Mucor Rouxii. FEMS Microbiol Lett. 1997 Oct 1;155(1):73-7. PubMed PMID: 9345767.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Function and regulation of the acid and neutral trehalases of Mucor rouxii. AU - de Almeida,F M, AU - Lúcio,A K, AU - Polizeli,M L, AU - Jorge,J A, AU - Terenzi,H F, PY - 1997/11/5/pubmed PY - 1997/11/5/medline PY - 1997/11/5/entrez SP - 73 EP - 7 JF - FEMS microbiology letters JO - FEMS Microbiol. Lett. VL - 155 IS - 1 N2 - Two different trehalose-hydrolysing activities, known as acid or non-regulatory trehalases, and neutral or regulatory trehalases, have been recognised in a number of fungal species. The true role of these apparently redundant hydrolases remained obscure for many years. However, recent evidence suggests that neutral trehalases would be specialised in the mobilisation of cytosolic trehalose, while acid trehalases would only hydrolyse extracellular trehalose. Results obtained with Mucor rouxii, a Zygomycete initially thought to possess only neutral trehalase activity, reinforced this hypothesis. M. rouxii grows efficiently in trehalose as the sole carbon source. Trehalose-grown or carbon-starved cells exhibit a high trehalase activity of optimum pH 4.5, bound to the external surface of the cell wall, in contrast with the neutral (pH 6.5) trehalase, which occurs in the cytosol. Other differences between the neutral and the acid trehalases are the temperature optimum (35 degrees C and 45 degrees C, respectively) and thermal stability (half-life of 2.5 min and 12 min at 45 degrees C, respectively). The neutral trehalase, but not the acid trehalase, is activated in vitro by cAMP-dependent phosphorylation, stimulated by Ca2+, and inhibited by EDTA. It shows maximal activity at germination and decreases as growth proceeds. In contrast the activity of the acid trehalase is totally repressed in glucose-grown cultures and increases upon exhaustion of the carbon source, and is strongly induced by extracellular trehalose. SN - 0378-1097 UR - https://www.unboundmedicine.com/medline/citation/9345767/Function_and_regulation_of_the_acid_and_neutral_trehalases_of_Mucor_rouxii_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.1997.tb12688.x DB - PRIME DP - Unbound Medicine ER -