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Updated: Aug 31, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Abstract:
Rafter, Gale W. (The Johns Hopkins School of Medicine and School of Hygiene and Public Health, Baltimore, Md.) and William C. Lane. Phosphoproteins in Escherichia coli. J. Bacteriol. 83:1077-1083. 1962.-The identification and metabolism of phosphoprotein were investigated in Escherichia coli. Hydrolysis of bacterial protein fractions with barium hydroxide or with phosphoprotein phosphatase released acid-soluble phosphorus. Chromatography of acid-hydrolyzed and incubated fractions also indicated the presence of phospho-amino acids. Turnover of phosphate in protein of growing cells was not observed, but incorporation of phosphate into protein of nongrowing cells was found. The protein-phosphate content decreased as organisms passed from the growing to the nongrowing state. The phosphoprotein composition, as revealed by paper electrophoresis, was heterogeneous. No protein phosphokinase or protein-phosphate phosphatase was detected in cell-free extracts, but an active principle which catalyzed the formation of acid-soluble phosphate from bacterial protein fractions was found.
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