Isolation of IIIGlc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium.

Journal of Bacteriology
B J ScholteP W Postma

Abstract

We report a procedure for the isolation of IIIglc of Salmonella typhimurium, a protein component of the phosphoenolpyruvate-dependent sugar phosphotransferase system. IIIGlc is a soluble protein with a molecular weight of 21,000, as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified protein is involved in the phosphoenolpyruvate-dependent phosphorylation of methyl alpha-glucoside in vitro. Its affinity for octyl-Sepharose may be an indication of the partial hydrophobic nature of IIIGlc. A specific antiserum against purified IIIGlc was prepared. Growth on different carbon sources did not affect the synthesis of IIIGlc, as determined by quantitative immunoelectrophoresis. Mutations which lower the adenosine 3',5'-phosphate level, such as cya and pts, do not alter the IIIGlc level. The closely related enteric bacteria Escherichia coli and Klebsiella aerogenes contain a protein factor which is closely related to IIIGlc of S. typhimurium, whereas Staphylococcus aureus does not.

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Citations

Jun 1, 1987·Biotechnology and Bioengineering·N G RayK Venkatasubramanian
Jan 1, 1983·Molecular & General Genetics : MGG·M L GlesynaV N Gershanovitch
Jan 1, 1986·Annals of the New York Academy of Sciences·N G RayK Venkatasubramanian
Jun 27, 1998·Molecular Microbiology·B M HogemaP W Postma
Jan 1, 1983·Molecular & General Genetics : MGG·W J DobrogoszT Melton
Sep 29, 2019·Research in Microbiology·Rebecca MächtelCédric Orelle
Sep 1, 1983·Microbiological Reviews·K E Sanderson, J R Roth
Sep 1, 1985·Microbiological Reviews·P W Postma, J W Lengeler
Sep 1, 1993·Microbiological Reviews·P W PostmaG R Jacobson

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