Amplification of the Streptococcus faecalis proton-translocating ATPase by a decrease in cytoplasmic pH.
When Streptococcus faecalis was grown in the presence of protonophores , an ATPase activity of the membrane was increased at a pH below 8.0 but not at a pH above 8.0. Characteristics of this increased ATPase were identical to those of a proton-translocating ATPase (H+-ATPase) located on the membrane of normal cells. The cytoplasmic pH was regulated at 7.6 to 7.8 but was not regulated in the presence of protonophores . The increase in the H+-ATPase was observed when the cytoplasmic pH was lowered to less than 7.6 by the addition of protonophores and was not related to the dissipation of the proton motive force. Thus, we suggest that the H+-ATPase of the membrane is amplified when the cytoplasmic pH is lowered below the pH at which it is regulated under normal conditions.
D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002462:Cell Membrane / Q000502:physiology; D003593:Cytoplasm / Q000378:metabolism; D013293:Enterococcus faecalis / Q000201:enzymology*; D006096:Gramicidin / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008564:Membrane Potentials; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D006096:Gramicidin; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D006180:Proton-Translocating ATPases