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Activation of the CheA kinase by asparagine in Bacillus subtilis chemotaxis

Department of Biochemistry, Colleges of Medicine and Liberal Arts and Sciences, University of Illinois, Urbana, IL 61801, USA

Author for correspondence: George W. Ordal. Tel: +1 217 333 9098. Fax: +1 217 333 8868 e-mail: G-Ordal@UIUC.EDU

ABSTRACT

Summary: Past experiments have shown that CheA and CheY are required to generate smooth swimming signals in Bacillus subtilis chemotaxis. This study, as anticipated from in vivo experiments, demonstrates in vitro that an attractant-bound chemoreceptor leads to an increase in CheA activity, which in turn leads to an increase in the Che Y-P pool that ultimately causes a behavioural change in the bacteria. Asparagine has been found to increase the rate of Che Y-P formation in the presence of McpB-containing membranes, CheA, and an excess of CheY. This asparagine effect requires the presence of both CheA and McpB, the latter of which has been shown to be the sole receptor for this attractant. Utilizing membranes from a number of B. subtilis null mutant strains, insight has also been gained into the potential roles of a number of unique chemotaxis proteins in the regulation of CheA activity in the presence and absence of this attractant.