Abstract
A mutant of Escherichia coli has been isolated, the growth of which is inhibited by low concentrations (1 mm) of NaCl. High levels of magnesium, calcium, or strontium in the medium permit growth in the presence of sodium. The metal content of the inhibited mutant is normal, but the strain is unable to tolerate levels of sodium to which the wild type is indifferent. Immediately after the addition of sodium to cultures of the mutant, rates of synthesis of protein, ribonucleic acid, deoxyribonucleic acid, and total lipid are unchanged, but more cardiolipin and less phosphatidylethanolamine are produced. The direct enzymatic cause of this change, which affects membrane function, is not known. Studies of the metabolism of phosphatidylglycerol in vivo after pulse-labeling with [2-3H]glycerol reveal that a major pathway both in wild-type and mutant strains involves the cleavage of labeled glycerol from phosphatidylglycerol.
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