PHOSPHORYLATED TYROSINE IN THE FLAGELLUM FILAMENT PROTEIN OF PSEUDOMONAS-AERUGINOSA

被引：41

作者：

KELLYWINTENBERG, K ^{[1
]}

ANDERSON, T ^{[1
]}

MONTIE, TC ^{[1
]}

机构：

[1] UNIV TENNESSEE, DEPT MICROBIOL, KNOXVILLE, TN 37996 USA

来源：

JOURNAL OF BACTERIOLOGY | 1990年 / 172卷 / 09期

关键词：

D O I：

10.1128/jb.172.9.5135-5139.1990

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：5135 / 5139

页数：5

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