Inhibition of elongation steps of protein synthesis at reduced potassium concentrations in reticulocytes and reticulocyte lysate.
We treated intact reticulocytes with nystatin to make them permeable to small cations and varied the concentration of K+ in the medium; the ionic strength was kept constant by adjusting Na+. As the intracellular K+ was lowered, the rate of protein synthesis decreased. In a reticulocyte lysate, the dependence of the rate of protein synthesis on K+ concentration (at constant ionic strength) was similar to that seen in nystatin-treated cells. We observed no loss of polysomes at low K+. Even when initiation was blocked with aurintricarboxylic acid, decreased K+ inhibited protein synthesis. Analysis of the kinetics of synthesis showed that lowering the K+ concentration inhibits the rate of elongation of nascent chains, but has little effect on the relative rate of initiation of chains.
D000818:Animals; D005914:Globins / Q000096:biosynthesis; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects*; D011188:Potassium / Q000494:pharmacology*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D012964:Sodium / Q000494:pharmacology
D005914:Globins; D012964:Sodium; D008274:Magnesium; D011188:Potassium