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Characterization of trehalase in Rhodotorula rubra.

J J Mansure1, J T Silva, A D Panek

  • 1Depart. de Bioquímica, Universidade Federal do Rio de Janeiro, Brasil.

Biochemistry International
|December 1, 1992
PubMed
Summary
This summary is machine-generated.

Trehalase in Rhodotorula rubra is particulate, unlike in Saccharomyces cerevisiae. Its activity is regulated by glucose repression and de novo synthesis, distinct from previously studied mechanisms.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Physiology

Background:

  • Trehalase is a key enzyme in trehalose metabolism, crucial for cellular stress response and energy storage in various organisms.
  • Understanding trehalase localization and regulation provides insights into yeast physiology and metabolic adaptability.
  • Previous studies on Saccharomyces cerevisiae indicate soluble trehalase, but less is known about Rhodotorula rubra's trehalase.

Purpose of the Study:

  • To characterize the trehalase activity in the yeast Rhodotorula rubra.
  • To investigate the subcellular localization and regulatory mechanisms of R. rubra trehalase.
  • To compare the properties of R. rubra trehalase with those of Saccharomyces cerevisiae.

Main Methods:

  • Preparation of cell-free extracts from Rhodotorula rubra.
  • Fractionation of cell extracts to determine enzyme localization (particulate vs. soluble).
  • Enzyme assays under various conditions (different carbon sources, presence of glucose, cycloheximide, cAMP-dependent protein kinase inhibitors).

Main Results:

  • Trehalase activity in Rhodotorula rubra was primarily associated with the particulate fraction, contrasting with the soluble trehalase in Saccharomyces cerevisiae.
  • Enzyme activity was strongly repressed by glucose and derepressed by maltose, trehalose, and glycerol.
  • Increased trehalase activity resulted from de novo synthesis, evidenced by cycloheximide inhibition, and catabolite inactivation by glucose was observed. The particulate enzyme was unresponsive to cAMP-dependent protein kinase activation.

Conclusions:

  • Rhodotorula rubra possesses a particulate trehalase with unique regulatory properties compared to Saccharomyces cerevisiae.
  • The regulation involves glucose repression, de novo synthesis, and catabolite inactivation, highlighting distinct metabolic control mechanisms.
  • The particulate nature and lack of cAMP-dependent kinase activation suggest novel pathways for trehalase regulation in this yeast species.