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Updated: Aug 2, 2025

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
F-type proton-pumping ATPase mediates acid tolerance in Streptococcus mutans
Mizuki Sekiya1, Kazuya Ikeda1, Ayaka Yonai1
1Division of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate 028-3694, Japan.
Aims:
Streptococcus mutans is highly sensitive to inhibitors of proton-pumping F-type ATPase (F-ATPase) under acidic conditions. Herein, we investigated the role of S. mutans F-ATPase in acid tolerance using a bacterium expressing the F-ATPase β subunit at lower levels than the wild-type strain.
Methods And Results:
We generated a mutant S. mutans expressing the catalytic β subunit of F-ATPase at lower levels than the wild-type bacterium. The mutant cells exhibited a significantly slower growth rate at pH 5.30, whereas the rate was essentially the same as that of wild-type cells at pH 7.40. In addition, the colony-forming ability of the mutant was decreased at pH <4.30 but not at pH 7.40. Thus, the growth rate and survival of S. mutans expressing low levels of the β subunit were reduced under acidic conditions.
Conclusions:
Together with our previous observations, this study indicates that F-ATPase is involved in the acid tolerance mechanism of S. mutans by secreting protons from the cytoplasm.
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