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Journal of Bacteriology, May 2006, p. 3487-3493, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3487-3493.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Signaling Interactions between the Aerotaxis Transducer Aer and Heterologous Chemoreceptors in Escherichia coli

Khoosheh K. Gosink, Maria del Carmen Burón-Barral, and John S. Parkinson*

Biology Department, University of Utah, Salt Lake City, Utah 84112

Received 6 February 2006/ Accepted 3 March 2006

Aer, a low-abundance signal transducer in Escherichia coli, mediates robust aerotactic behavior, possibly through interactions with methyl-accepting chemotaxis proteins (MCP). We obtained evidence for interactions between Aer and the high-abundance aspartate (Tar) and serine (Tsr) receptors. Aer molecules bearing a cysteine reporter diagnostic for trimer-of-dimer formation yielded cross-linking products upon treatment with a trifunctional maleimide reagent. Aer also formed mixed cross-linking products with a similarly marked Tar reporter. An Aer trimer contact mutation known to abolish trimer formation by MCPs eliminated Aer trimer and mixed trimer formation. Trimer contact alterations known to cause epistatic behavior in MCPs also produced epistatic properties in Aer. Amino acid replacements in the Tar trimer contact region suppressed an epistatic Aer signaling defect, consistent with compensatory conformational changes between directly interacting proteins. In cells lacking MCPs, Aer function required high-level expression, comparable to the aggregate number of receptors in a wild-type cell. Aer proteins with clockwise (CW)-biased signal output cannot function under these conditions but do so in the presence of MCPs, presumably through formation of mixed signaling teams. The Tar signaling domain was sufficient for functional rescue. Moreover, CW-biased lesions did not impair aerotactic signaling in a hybrid Aer-Tar transducer capable of adjusting its steady-state signal output via methylation-dependent sensory adaptation. Thus, MCPs most likely assist mutant Aer proteins to signal productively by forming collaborative signaling teams. Aer evidently evolved to operate collaboratively with high-abundance receptors but can also function without MCP assistance, provided that it can establish a suitable prestimulus swimming pattern.

* Corresponding author. Mailing address: Biology Department, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112. Phone: (801) 581-7639. Fax: (801) 581-4668. E-mail: Parkinson{at}biology.utah.edu.

Journal of Bacteriology, May 2006, p. 3487-3493, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3487-3493.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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