Summary
2-ketobutyrate and its analogues were found to inhibit strongly and transiently the rate of β-galactosidase synthesis in Escherichia coli K12. This effect was ascribed to a strong and transient inhibition of the adenylate cyclase activity. By using pts mutants, we showed, in agreement with our previous results (Daniel et al. 1983), that the likely target of 2-ketobutyrate and its analogues is the phosphoenolpyruvate: glycose phosphotransferase transport system (PTS). Furthermore, evidence for such a cascade effect caused by 2-ketobutyrate and its analogues allowed us to corroborate our previous proposal (Daniel et al. 1983) that 2-ketobutyrate, a precursor of isoleucine, acts as an E. coli alarmone monitoring the passage from anaerobic to aerobic growth conditions.
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Communicated by G.A. O'Donovan
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Daniel, J., Joseph, E. & Danchin, A. Role of 2-ketobutyrate as an alarmone in E. coli K12: Inhibition of adenylate cyclase activity mediated by the phosphoenolpyruvate: Glycose phosphotransferase transport system. Molec. Gen. Genet. 193, 467–472 (1984). https://doi.org/10.1007/BF00382085
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DOI: https://doi.org/10.1007/BF00382085