Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system

FEBS Letters

Rowsell, Edward H.¹  Taylor, Barry L.¹  Johnson, Mark S.¹ 

[1] Department of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350, USA

关键词: Bacterial chemotaxis;    Phosphotransferase system;    Enzyme I;    CheA protein;    CheY protein;    Acetate kinase;    Escherichia coli;   

DOI  :  10.1016/0014-5793(95)01097-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II^mtl of the PTS with [γ-³²P]ATP or [³²P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems.

【 授权许可】

Unknown