Abstract
Both a- and b-type purified flagellins from a number of Pseudomonas aeruginosa strains grown in radiolabeled phosphate were shown to be phosphorylated. Analysis of partial acid-hydrolyzed flagellar filaments revealed that 32Pi was in phosphotyrosine. Three 32P-phosphopeptides apparently are common to a- and b-type flagellins, but a fourth peptide was found only in b-type hydrolysates. P. aeruginosa PAK flagellin, containing only two tyrosines, both in the variable region, was readily labeled and gave the same peptide pattern as flagellins containing additional tyrosines. Data showing that a- and b-type flagellins gave positive immunoblots with antiphosphotyrosine monoclonal antibody and that release of P(i) by alkaline phosphatase occurred indicated that unmodified tyrosine phosphate exists in flagellin.
MeSH Terms
Antibodies, Monoclonal/immunology
Flagella/metabolism
Flagellin/chemistry,isolation & purification
Immunoblotting
Phosphoric Monoester Hydrolases/metabolism
Phosphorylation
Phosphotyrosine
Pseudomonas aeruginosa/chemistry,metabolism
Trypsin/pharmacology
Tyrosine/analogs & derivatives,analysis
Chemicals
Antibodies, Monoclonal
Flagellin
Phosphotyrosine
Tyrosine
Phosphoric Monoester Hydrolases
Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kelly-Wintenberg K
Department of Microbiology, University of Tennessee, Knoxville 37996.
South S L
Montie T C
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