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J. Biol. Chem., Vol. 279, Issue 46, 48152-48158, November 12, 2004

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The HAMP Linker in Histidine Kinase Dimeric Receptors Is Critical for Symmetric Transmembrane Signal Transduction^*

Yan Zhu and Masayori Inouye

From the Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

The HAMP linker, a common structural element between a sensor and a transmitter module in various sensor proteins, plays an essential role in signal transduction. Here, by in vivo complementation experiments with Tar-EnvZ hybrid receptor mutants in which the HAMP linker forms a heterodimer with Tar and EnvZ-type subunits, we found that mutations at one linker only affect the function of EnvZ in the same subunit. However, the same mutations affect the EnvZ function of both subunits when only a Tar or EnvZ-type HAMP linker is used. These results suggest that intersubunit interactions in the HAMP linker normally mediate signal transduction through both subunits in a sensor dimer, whereas the signal is asymmetrically transduced through the linker in a heterodimer. This is the first demonstration that two HAMP linkers in a sensor dimer are functionally coupled for normal signal transduction; however, this functional coupling can be reduced when the HAMP linkers lose their symmetric nature.

Received for publication, January 29, 2004 , and in revised form, July 26, 2004.

^* This work was supported by National Institutes of Health Grant GM19043. 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.

To whom correspondence should be addressed. Tel.: 732-235-4115; Fax: 732-235-4559; E-mail: inouye{at}rwja.umdnj.edu.

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