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Amplification of the Streptococcus faecalis proton-translocating ATPase by a decrease in cytoplasmic pH.

H Kobayashi, T Suzuki, N Kinoshita

    Journal of Bacteriology
    |June 1, 1984
    PubMed
    Summary

    Protonophores increase membrane ATPase activity in Streptococcus faecalis when cytoplasmic pH drops below 7.6. This suggests proton-translocating ATPase (H+-ATPase) is amplified to regulate internal pH.

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    Area of Science:

    • Microbiology
    • Cellular Physiology
    • Biochemistry

    Background:

    • Streptococcus faecalis regulates cytoplasmic pH (pHc) within a narrow range (7.6-7.8).
    • Membrane-bound proton-translocating ATPase (H+-ATPase) plays a role in maintaining pH homeostasis.

    Purpose of the Study:

    • To investigate the effect of protonophores on membrane ATPase activity and pH regulation in Streptococcus faecalis.
    • To determine if H+-ATPase is involved in response to altered cytoplasmic pH.

    Main Methods:

    • Growth of Streptococcus faecalis in the presence of protonophores.
    • Measurement of membrane ATPase activity at different external pH levels.
    • Monitoring of cytoplasmic pH regulation.

    Main Results:

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    • Protonophores increased membrane ATPase activity significantly at pH below 8.0, but not above.
    • The characteristics of the induced ATPase matched the native H+-ATPase.
    • Cytoplasmic pH regulation failed in the presence of protonophores.
    • Increased H+-ATPase activity correlated with a drop in cytoplasmic pH below 7.6, independent of proton motive force dissipation.

    Conclusions:

    • The H+-ATPase of Streptococcus faecalis is amplified in response to a lowered cytoplasmic pH.
    • This amplification mechanism appears to be a direct response to intracellular acidity rather than a consequence of altered proton motive force.
    • The findings suggest a specific regulatory role for H+-ATPase in maintaining cytoplasmic pH homeostasis under stress conditions.