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Peptide transport in Candida albicans.
Journal of General Microbiology
|September 1, 1979
Summary
Candida albicans utilizes a specific, saturable system for trimethionine uptake, which is energy-dependent and pH-sensitive. Once inside, trimethionine is quickly broken down by a peptidase.
Area of Science:
- Mycology
- Biochemistry
- Cell Biology
Background:
- Candida albicans is an opportunistic fungal pathogen.
- Understanding nutrient uptake mechanisms is crucial for developing targeted antifungal strategies.
Purpose of the Study:
- To investigate the uptake mechanism of trimethionine in Candida albicans.
- To characterize the kinetic and regulatory properties of this transport system.
Main Methods:
- Utilizing radiolabeled trimethionine (L-methionyl-L-methionyl-L-[METHYL-14C]methionine) for uptake studies.
- Assessing the effects of pH, temperature, metabolic inhibitors, and competing peptides on uptake.
- Analyzing the intracellular fate of trimethionine.
Main Results:
- Trimethionine uptake is mediated by a saturable system with specific pH (3.5) and temperature (37°C) optima and an apparent Km of 3.3 x 10^-5 M.
- Uptake is energy-dependent, as indicated by inhibition with sodium azide and dinitrophenol.
- Structural analogs like (Leu)3 and Gly-Met-Gly competed for uptake, while methionine and dimethionine did not, suggesting specificity.
- Trimethionine is rapidly hydrolyzed by a peptidase post-internalization.
Conclusions:
- Candida albicans possesses a distinct, high-affinity transport system for trimethionine.
- This uptake mechanism is active and specific, differentiating trimethionine from smaller methionine-containing peptides.
- The rapid intracellular hydrolysis suggests a role for trimethionine as a source of methionine or its derivatives within the cell.