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Originally published In Press as doi:10.1074/jbc.M600018200 on May 4, 2006

J. Biol. Chem., Vol. 281, Issue 33, 23880-23886, August 18, 2006
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Control of Chemotactic Signal Gain via Modulation of a Pre-formed Receptor Array*Formula

Hiroki Irieda{ddagger}, Motohiro Homma{ddagger}1, Michio Homma{ddagger}, and Ikuro Kawagishi{ddagger}§2

From the {ddagger}Division of Biological Science, Graduate School of Science, and §Institute for Advanced Research, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan

The remarkably wide dynamic range of the chemotactic pathway of Escherichia coli, a model signal transduction system, is achieved by methylation/amidation of the transmembrane chemoreceptors that regulate the histidine kinase CheA in response to extracellular stimuli. The chemoreceptors cluster at a cell pole together with CheA and the adaptor CheW. Several lines of evidence have led to models that assume high cooperativity and sensitivity via collaboration of receptor dimers within a cluster. Here, using in vivo disulfide cross-linking assays, we have demonstrated a well defined arrangement of the aspartate chemoreceptor (Tar). The differential effects of amidation on cross-linking at different positions indicate that amidation alters the relative orientation of Tar dimers to each other (presumably inducing rotational displacements) without much affecting the conformation of the periplasmic domains. Interestingly, the effect of aspartate on cross-linking at any position tested was roughly opposite to that of receptor amidation. Furthermore, amidation attenuated the effects of aspartate by several orders of magnitude. These results suggest that receptor covalent modification controls signal gain by altering the arrangement or packing of receptor dimers in a pre-formed cluster.


Received for publication, January 3, 2006 , and in revised form, May 4, 2006.

* This work was supported in part by grants-in-aid for scientific research from the Japan Society for the Promotion of Science and from the Institute for Advanced Research, Nagoya University (to I. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental videos S1 and S2.

1 Present address: Dept. of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, 3-8-1 Komaba, Meguro, Tokyo 153-8902, Japan.

2 To whom correspondence should be addressed. Tel.: 81-52-789-2993; Fax: 81-52-789-3001; E-mail: i45406a{at}cc.nagoya-u.ac.jp.


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