Abstract
The C-terminal domain of subunit ε of the bacterial FoF1 ATP synthase is reported to be an intrinsic inhibitor of ATP synthesis/hydrolysis activity in vitro, preventing wasteful hydrolysis of ATP under low-energy conditions. Mutants defective in this regulatory domain exhibited no significant difference in growth rate, molar growth yield, membrane potential, or intracellular ATP concentration under a wide range of growth conditions and stressors compared to wild-type cells, suggesting this inhibitory domain is dispensable for growth and survival of Escherichia coli.
Original language | English (US) |
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Pages (from-to) | 2046-2052 |
Number of pages | 7 |
Journal | Journal of Bacteriology |
Volume | 193 |
Issue number | 8 |
DOIs |
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State | Published - Apr 2011 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Molecular Biology