Phosphorylated tyrosine in the flagellum filament protein of Pseudomonas aeruginosa.
Purified flagella from two strains of 32P-labeled Pseudomonas aeruginosa were shown to be phosphorylated. This was confirmed by autoradiography of flagellin protein in polyacrylamide gels. Thin-layer electrophoresis and autoradiography of flagellin partial hydrolysates indicated that phosphotyrosine was the major phosphorylated amino acid. High-pressure liquid chromatographic analysis confirmed the presence of phosphotyrosine in flagellum filament protein. Preliminary data indicated that less than one tyrosine per subunit was phosphorylated. No evidence was found for phosphorylation of serine or threonine. A function related to tyrosine phosphorylation has not been determined.
Department of Microbiology, University of Tennessee, Knoxville 37996.
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Kelly-Wintenberg
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Anderson
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Montie
D001345:Autoradiography; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002458:Cell Fractionation / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005407:Flagella / Q000032:analysis* / Q000648:ultrastructure; D005408:Flagellin / Q000302:isolation & purification*; D015151:Immunoblotting; D008970:Molecular Weight; D010761:Phosphorus Radioisotopes; D019000:Phosphotyrosine; D011550:Pseudomonas aeruginosa / Q000032:analysis*; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis
D001426:Bacterial Proteins; D010761:Phosphorus Radioisotopes; D005408:Flagellin; D019000:Phosphotyrosine; D014443:Tyrosine