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H+-Translocating Membrane-Bound Pyrophosphatase from Rhodospirillum rubrum Fuels Escherichia coli Cells via an Alternative Pathway for Energy Generationстатья
- Авторы: Malykh E.A., Golubeva L.I., Kovaleva E.S., Shupletsov M.S., Rodina E.V., Mashko S.V., Stoynova N.V.
- Журнал: Microorganisms
- Том: 11
- Номер: 2
- Год издания: 2023
- Издательство: MDPI
- Местоположение издательства: Basel, Switzerland
- Первая страница: 294
- Последняя страница: 10
- DOI: 10.3390/microorganisms11020294
- Аннотация: Inorganic pyrophosphatases (PPases) catalyze an essential reaction, namely, the hydrolysis of PPi, which is formed in large quantities as a side product of numerous cellular reactions. In the majority of living species, PPi hydrolysis is carried out by soluble cytoplasmic PPase (S-PPases) with the released energy dissipated in the form of heat. In Rhodospirillum rubrum, part of this energy can be conserved by proton-pumping pyrophosphatase (H+-PPaseRru) in the form of aproton electrochemical gradient for further ATP synthesis. Here, the codon-harmonized gene hppaRru encoding H+-PPaseRru was expressed in the Escherichia coli chromosome. We demonstrate, for the first time, that H+-PPaseRru complements the essential native S-PPase in E. coli cells. 13C-MFA confirmed that replacing native PPase to H+-PPaseRru leads to the re-distribution of carbon fluxes; a statistically significant 36% decrease in tricarboxylic acid (TCA) cycle fluxes was found compared with wild-type E. coli MG1655. Such a flux re-distribution can indicate the presence of an additional method for energy generation (e.g., ATP), which can be useful for the microbiological production of a number ofcompounds, the biosynthesis of which requires the consumption of ATP.
- Добавил в систему: Родина Елена Валерьевна