Uptake of gentamicin by Staphylococcus aureus possessing gentamicin-modifying enzymes: enhancement of uptake by puromycin and N,N'-dicyclohexylcarbodiimide.
Uptake of gentamicin by a gentamicin-resistant strain of Staphylococcus aureus possessing the aminoglycoside-modifying phosphotransferase enzyme APH(2") was enhanced by the protein synthesis inhibitor, puromycin or by the proton-translocating ATPase inhibitor, N,N'-dicylohexylcarbodiimide. Such enhanced uptake was inhibited by carbonyl cyanide p trifluoromethoxyphenylhydrazone or by valinomycin in the presence of potassium ions, suggesting a role for the transmembrane proton motive force in the process. The accumulated gentamicin did not cause loss of cell viability and exhibited altered chromatographic mobility compared with a control (unmodified) preparation of gentamicin.
D002234:Carbodiimides / Q000494:pharmacology*; D002854:Chromatography, Paper; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D004352:Drug Resistance, Microbial; D005839:Gentamicins / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism; D011188:Potassium / Q000494:pharmacology; D011691:Puromycin / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000201:enzymology / Q000378:metabolism*
D002234:Carbodiimides; D005839:Gentamicins; D011691:Puromycin; D004024:Dicyclohexylcarbodiimide; D010770:Phosphotransferases; D011188:Potassium