Competition between Two Pathways for Sugar Uptake by the Phosphoenolpyruvate-Dependent Sugar Phosphotransferase System in Salmonella typhimurium

2005 ◽  
Vol 114 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Bob J. SCHOLTE ◽  
Pieter W. POSTMA
1983 ◽  
Vol 61 (2-3) ◽  
pp. 150-153 ◽  
Author(s):  
E. Bruce Waygood ◽  
Roshan L. Mattoo

A protein has been found by isoelectricfocusing and autoradiography in Escherichia coli and Salmonella typhimurium which was phosphorylated by enzyme I and an histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate–sugar phosphotransferase system (PTS). This protein was not factor IIIglc nor was it specifically induced by fructose. Its presence in soluble crude extracts was dependent upon growth conditions; however, the two bacteria had different patterns and amounts in respect to this novel protein. The protein was present in S. typhimurium SB2950 which has an extensive deletion through the pts operon, thus indicating that it must be coded for elsewhere on the genome.


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