Role of 2-ketobutyrate as an alarmone in E. coli K12: Inhibition of adenylate cyclase activity mediated by the phosphoenolpyruvate: Glycose phosphotransferase transport system
✍ Scribed by Daniel, Jacques ;Joseph, Evelyne ;Danchin, Antoine
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 567 KB
- Volume
- 193
- Category
- Article
- ISSN
- 0026-8925
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✦ Synopsis
2-ketobutyrate and its analogues were found to inhibit strongly and transiently the rate of beta-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.