Properties of three distinct pyrimide transport systems in yeast. Evidence for distinct energy coupling.
In Saccharomyces cerevisiae the uptake of cytosine, uracil and uridine is mediated by three permeases. Using mutants blocked in the metabolic utilization of these three compounds we were able to study their specific uptake. Cytosine and uridine show simple saturation kinetics, whereas uracil uptake is a biphasic process. A comparison of the effects of several inhibitors of energy metabolism on these uptake systems was made. Striking differences were found. 2,4-Dinitrophenol (10(-3) M) and NaN3 (10(-2) M) inhibit the entry of the three compounds to similar extent, but chlorhexidine (10(-5) M) and Dio 9 (50 microgram/ml) which are ATPase inhibitors in vitro strongly impaired cytosine and uridine entry and remained without effect on uracil uptake. We provisionally conclude that these systems may be energized by different mechanisms. In the case of cytosine and uridine permease, a membrane ATPase is possibly involved in the process of energetic coupling whereas this does not seem to be so for uracil.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001386:Azides / Q000494:pharmacology; D001693:Biological Transport, Active / Q000187:drug effects; D002710:Chlorhexidine / Q000494:pharmacology; D003596:Cytosine / Q000378:metabolism; D004140:Dinitrophenols / Q000494:pharmacology; D007700:Kinetics; D026901:Membrane Transport Proteins / Q000378:metabolism; D011743:Pyrimidines / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D014498:Uracil / Q000378:metabolism; D014529:Uridine / Q000378:metabolism
D001386:Azides; D004140:Dinitrophenols; D026901:Membrane Transport Proteins; D011743:Pyrimidines; D014498:Uracil; D003596:Cytosine; D000251:Adenosine Triphosphatases; D002710:Chlorhexidine; D014529:Uridine