The ‘CheA’ and ‘CheY’ domains of Myxococcus xanthus FrzE function independently in vitro as an autokinase and a phosphate acceptor, respectively

FEBS Letters

Acuña, Gonzalo¹  Zusman, David R.¹  Shi, Wenyuan¹  Trudeau, Kathy¹ 

[1] Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720, USA

关键词: Chemotaxis;    Signal transduction;    Two-component system;    frz;    Myxococcus xanthus;   

DOI  :  10.1016/0014-5793(94)01389-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

FrzE is a chemotaxis protein in Myxococcus xanthus which has sequence homology to two different chemotaxis proteins of enteric bacteria, CheA (autokinase) and CheY (phosphate acceptor) [Proc. Natl. Acad. Sci. USA 87 (1990) 5898–5902]. It was also shown that a recombinant FrzE protein was autophosphorylated when incubated in the presence of ATP and Mn²⁺ [J. Bacteriol. 172 (1990) 6661–6668]. In this study, we further investigated the biochemical properties of FrzE. Two recombinant proteins were produced: one containing only the ‘CheA’ domain of FrzE and the second only the ‘CheY’ domain. The CheA domain polypeptide contained the autokinase activity which was absent from the CheY domain polypeptide. The phosphorylated CheA domain polypeptide as well as the intact FrzE protein were able to transfer phosphate groups to the CheY domain peptide. These results indicate that FrzE has structural as well as functional homologies to CheA and CheY in a single polypeptide.

【 授权许可】

Unknown