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Journal of Bacteriology, April 2001, p. 2204-2211, Vol. 183, No. 7
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.7.2204-2211.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Genetic Evidence that the alpha 5 Helix of the Receiver Domain of PhoB Is Involved in Interdomain Interactions

Mindy P. Allen, Kimberly B. Zumbrennen,dagger and William R. McCleary*

Microbiology Department, Brigham Young University, Provo, Utah 84602-5253

Received 8 November 2000/Accepted 12 January 2001

Two-component signaling proteins are involved in transducing environmental stimuli into intracellular signals. Information is transmitted through a phosphorylation cascade that consists of a histidine protein kinase and a response regulator protein. Generally, response regulators are made up of a receiver domain and an output domain. Phosphorylation of the receiver domain modulates the activity of the output domain. The mechanisms by which receiver domains control the activities of their respective output domains are unknown. To address this question for the PhoB protein from Escherichia coli, we have employed two separate genetic approaches, deletion analysis and domain swapping. In-frame deletions were generated within the phoB gene, and the phenotypes of the mutants were analyzed. The output domain, by itself, retained significant ability to activate transcription of the phoA gene. However, another deletion mutant that contained the C-terminal alpha -helix of the receiver domain (alpha 5) in addition to the entire output domain was unable to activate transcription of phoA. This result suggests that the alpha 5 helix of the receiver domain interacts with and inhibits the output domain. We also constructed two chimeric proteins that join various parts of the chemotaxis response regulator, CheY, to PhoB. A chimera that joins the N-terminal ~85% of CheY's receiver domain to the beta 5-alpha 5 loop of PhoB's receiver domain displayed phosphorylation-dependent activity. The results from both sets of experiments suggest that the regulation of PhoB involves the phosphorylation-mediated modulation of inhibitory contacts between the alpha 5 helix of its unphosphorylated receiver domain and its output domain.

* Corresponding author. Mailing address: Microbiology Department, Brigham Young University, 775 WIDB, Provo, UT 84602-5253. Phone: (801) 378-8793. Fax: (801) 378-9197. E-mail: bill_mccleary{at}byu.edu.

dagger Present address: University of Utah, Huntsman Cancer Institute, Salt Lake City, UT 84101.

Journal of Bacteriology, April 2001, p. 2204-2211, Vol. 183, No. 7
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.7.2204-2211.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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