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J. Biol. Chem., Vol. 281, Issue 10, 6768-6775, March 10, 2006

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Identification of a Ubiquinone-binding Site That Affects Autophosphorylation of the Sensor Kinase RegB^*

Lee R. Swem, Xing Gong, Chang-An Yu, and Carl E. Bauer¹

From the Department of Biology, Indiana University, Bloomington, Indiana 47405 and the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078

Rhodobacter capsulatus regulates many metabolic processes in response to the level of environmental oxygen and the energy state of the cell. One of the key global redox regulators of the cell's metabolic physiology is the sensor kinase RegB that controls the synthesis of numerous energy generation and utilization processes. In this study, we have succeeded in purifying full-length RegB containing six transmembrane-spanning elements. Exogenous addition of excess oxidized coenzyme Q₁ is capable of inhibiting RegB autophosphorylation 6-fold. However, the addition of reduced coenzyme Q₁ exhibits no inhibitory effect on kinase activity. A ubiquinone-binding site, as defined by azidoquinone photo affinity cross-linking, was determined to lie within a periplasmic loop between transmembrane helices 3 and 4 that contains a fully conserved heptapeptide sequence of GGXXNPF. Mutation of the phenylalanine in this heptapeptide renders RegB constitutively active in vivo, indicating that this domain is responsible for sensing the redox state of the ubiquinone pool and subsequently controlling RegB autophosphorylation.

Received for publication, September 2, 2005 , and in revised form, December 12, 2005.

^* This work was supported by National Institutes of Health Grants GM30721 (to C.-A. Y.) and GM53940 (to C. E. B.). 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.

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

¹ To whom correspondence should be addressed. Tel.: 812-855-6595; Fax: 812-856-4178; E-mail: cbauer{at}bio.indiana.edu.

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