pH regulation by Streptococcus mutans.

Abstract

The intracellular pH (pHi) optimum for glycolysis in Streptococcus mutans Ingbritt was determined to be 7.0 by use of the ionophore gramicidin for manipulation of pHi. Glycolytic activity decreased to zero as the pHi was lowered from 7.0 to 5.0. In contrast, glycolysis had an extracellular pH (pHo) optimum of 6.0 with a much broader profile. The relative insensitivity of glycolysis to the lowering of pHo was attributed to the ability of S. mutans to maintain a transmembrane pH gradient (delta pH, inside more alkaline) at low pHo. At a pHo of 5.0, glycolyzing cells of S. mutans maintained a delta pH of 1.37 +/- 0.09 units. The maintenance of this delta pH was dependent on the concentration of potassium ions in the extracellular medium. Potassium was rapidly taken up by glycolyzing cells of S. mutans at a rate of 70 nmol/mg dry weight/min. This uptake was dependent on the presence of both ATP and a proton motive-force (delta p). The addition of N-N'-dicyclohexylcarbodiimide (DCCD) to glycolyzing cells of S. mutans caused a partial collapse of the delta pH. Growth of S. mutants at pHo 5.5 in continuous culture resulted in the maintenance of a delta pH larger than that produced by cells grown at pH 7.0. These results suggest the presence of a proton-translocating F1Fo-ATPase in S. mutans whose activity is regulated by the intracellular pH and transmembrane electrical potential (delta psi). The production of an artificial delta p of 124 mV across the cell membrane of S. mutans did not result in proton movement through the F1Fo-ATPase coupled to ATP synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)