Abstract
The characteristics of the basic amino acid permease (system VI) of the filamentous fungus Penicillium chrysogenum were studied in plasma membranes fused with liposomes containing the beef heart mitochondrial cytochrome c oxidase. In the presence of reduced cytochrome c, the hybrid membranes accumulated the basic amino acids arginine and lysine. Inhibition studies with analogs revealed a narrow substrate specificity. Within the external pH range of 5.5 to 7.5, the transmembrane electrical potential (Δψ) functions as the main driving force for uphill transport of arginine, although a low level of uptake was observed when only a transmembrane pH gradient was present. It is concluded that the basic amino acid permease is a H+ symporter. Quantitative analysis of the steady-state levels of arginine uptake in relation to the proton motive force suggests a H+-arginine symport stoichiometry of one to one. Efflux studies demonstrated that the basic amino acid permease functions in a reversible manner.
| Original language | English |
|---|---|
| Pages (from-to) | 3991 - 3995 |
| Number of pages | 5 |
| Journal | Journal of Bacteriology |
| Volume | 178 |
| Issue number | 14 |
| Publication status | Published - Jul-1996 |
Keywords
- PROTON-MOTIVE FORCE
- CYTOCHROME-C
- BACTERIA
- OXIDASE
- SYSTEMS