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GAP1 activity is dependent on cAMP in Saccharomyces cerevisiae
A A Amitrano1, D A Saenz, E H Ramos
1Departamento de Bioquímica, Facultad de Medicina, Universidad de Buenos Aires-CONICET, Argentina.
FEMS Microbiology Letters
|June 15, 1997
Summary
Lowering cyclic AMP (cAMP) levels in yeast reduces the activity of the general amino acid permease (GAP1). This impacts the cell's ability to transport amino acids like L-citrulline.
Area of Science:
- Cellular biology
- Biochemistry
- Yeast genetics
Background:
- General amino acid permease (GAP1) is crucial for nutrient uptake in yeast.
- Cyclic AMP (cAMP) is a key second messenger regulating various cellular processes.
Purpose of the Study:
- To investigate the direct effect of cyclic AMP (cAMP) levels on the activity of the general amino acid permease (GAP1).
Main Methods:
- Utilized adenylate cyclase-deficient Saccharomyces cerevisiae strains.
- Evaluated GAP1 activity by measuring L-citrulline uptake rates.
- Performed kinetic analysis of the amino acid transport system.
Main Results:
- Decreased intracellular cAMP concentrations led to reduced initial rates of L-citrulline uptake.
- Kinetic studies indicated a partial loss of transport capacity.
- No significant changes in permease affinity for amino acids were observed.
Conclusions:
- Cyclic AMP (cAMP) levels play a regulatory role in general amino acid permease (GAP1) activity.
- Reduced cAMP negatively impacts the transport capacity of GAP1.
- GAP1 function is modulated by cAMP signaling pathways, affecting amino acid transport.