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Carbohydrate transport and cyclic 3′,5′ adenosine monophosphate (cAMP) levels in a temperature sensitive phosphotransferase mutant of Escherichia coli

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Summary

An E. coli mutant with a temperature sensitive enzyme I of the phosphoenolpyruvate dependent transferase system (PTS) is described. Its phenotype at 41° C is Mtl− Glu± Fru− Man− Lac− Glp− Mal− Ara+ Gal+; at 28°C, wild type. The half-life of the enzyme in extracts is 1.5–2.0 minutes at 41°C. The cellular content of 3′,5′ cyclic adenosine monophosphate (cAMP) in this mutant was measured and was the same at both temperatures. It is concluded that the effect of loss of enzyme I on the utilization of lactose1, maltose, and glycerol is not mediated through cellular cAMP levels. The mutant was used to study carbohydrate uptake and it was found that destruction of enzyme I by heating affected the uptake of those carbohydrates phosphorylated by the PTS but did not significantly affect the uptake of carbohydrates not phosphorylated by the PTS.

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Authors and Affiliations

  1. Department of Biophysics and Genetics, Webb-Waring Lung Institute, University of Colorado Medical Center, Denver, Colorado

    Rolf Dahl, Helvise G. Morse & M. L. Morse

Authors
  1. Rolf Dahl
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  2. Helvise G. Morse
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  3. M. L. Morse
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Additional information

Communicated by W. Arber

Grant support: NSF grant GB-24844, “Genetic Study of Metabolic Regulation”. Life Insuranco Medical Research Fund grant G69-23, “Molecular Basis of Carbohydrate Transport in Staphylococcus aureus”.

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Dahl, R., Morse, H.G. & Morse, M.L. Carbohydrate transport and cyclic 3′,5′ adenosine monophosphate (cAMP) levels in a temperature sensitive phosphotransferase mutant of Escherichia coli . Molec. Gen. Genet. 129, 1–10 (1974). https://doi.org/10.1007/BF00269261

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  • DOI: https://doi.org/10.1007/BF00269261

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