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Journal of Bacteriology, December 2001, p. 6807-6814, Vol. 183, No. 23
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.23.6807-6814.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The Default State of the Membrane-Localized Histidine Kinase PrrB of Rhodobacter sphaeroides 2.4.1 Is in the Kinase-Positive Mode

Jeong-Il Oh, In-Jeong Ko, and Samuel Kaplan*

Department of Microbiology and Molecular Genetics, Medical School, The University of Texas Health Science Center, Houston, Texas 77030

Received 23 March 2001/Accepted 27 August 2001

The PrrBA two-component activation system of Rhodobacter sphaeroides plays a major role in the induction of photosynthesis gene expression under oxygen-limiting or anaerobic conditions. The PrrB histidine kinase is composed of two structurally identifiable regions, the conserved C-terminal kinase/phosphatase domain and the N-terminal membrane-spanning domain with six transmembrane helices framing three periplasmic and two cytoplasmic loops. Using a set of PrrB mutants with lesions in the transmembrane domain, we demonstrate that the central portion of the PrrB transmembrane domain including the second periplasmic loop plays an important role in both sensing and signal transduction. Signal transduction via the transmembrane domain is ultimately manifested by controlling the activity of the C-terminal kinase/phosphatase domain. The extent of signal transduction is determined by the ability of the transmembrane domain to sense the strength of the inhibitory signal received from the cbb3 terminal oxidase (J.-I Oh, and S. Kaplan, EMBO J. 19:4237-4247, 2000). Therefore, the intrinsic ("default") state of PrrB is in the kinase-dominant mode. It is also demonstrated that the extent of prrB gene expression is subject to the negative autoregulation of the PrrBA system.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, The University of Texas Health Science Center, Medical School, 6431 Fannin, Houston, TX 77030. Phone: (713) 500-5502. Fax: (713) 500-5499. E-mail: samuel.kaplan{at}uth.tmc.edu.

Journal of Bacteriology, December 2001, p. 6807-6814, Vol. 183, No. 23
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.23.6807-6814.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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