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Journal of Bacteriology, April 2008, p. 2422-2433, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01827-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Analysis of the Campylobacter jejuni FlgR Response Regulator Suggests Integration of Diverse Mechanisms To Activate an NtrC-Like Protein{triangledown}

Stephanie N. Joslin and David R. Hendrixson*

Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390

Received 19 November 2007/ Accepted 12 January 2008

Flagellar motility in Campylobacter jejuni mediates optimal interactions with human or animal hosts. {sigma}54 and the FlgSR two-component system are necessary for the expression of many C. jejuni flagellar genes. The FlgR response regulator is homologous to the NtrC family of transcriptional activators. These regulators usually contain an N-terminal receiver domain, a central domain that interacts with {sigma}54 and hydrolyzes ATP, and a DNA-binding C-terminal domain. Most often, phosphorylation of the receiver domain influences its inherent ability to either positively or negatively control the activity of the regulator. In this study, we performed genetic and biochemical analyses to understand how FlgR activity is controlled to culminate in the expression of {sigma}54-dependent flagellar genes. Our data suggest that the FlgR receiver domain has the capacity for both positive and negative regulation in controlling the activation of the protein. Analysis of the C-terminal domain of FlgR revealed that it lacks a DNA-binding motif and is not required for {sigma}54-dependent flagellar gene expression. Further analysis of FlgR lacking the C-terminal domain indicates that this protein is partially functional in the absence of the cognate sensor kinase, FlgS, but its activity is still dependent on the phosphorylated residue in the receiver domain, D51. We hypothesize that the C-terminal domain may not function to bind DNA but may ensure the specificity of the phosphorylation of FlgR by FlgS. Our results demonstrate that FlgR activation mechanisms are unusual among characterized NtrC-like proteins and emphasize that various means are utilized by the NtrC family of proteins to control the transcription of target genes.

* Corresponding author. Mailing address: University of Texas Southwestern Medical School, Department of Microbiology, 5323 Harry Hines Boulevard, Dallas, TX 75390-9048. Phone: (214) 648-5949. Fax: (214) 648-5907. E-mail: david.hendrixson{at}utsouthwestern.edu

{triangledown} Published ahead of print on 25 January 2008.

Journal of Bacteriology, April 2008, p. 2422-2433, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01827-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Balaban, M., Joslin, S. N., Hendrixson, D. R. (2009). FlhF and Its GTPase Activity Are Required for Distinct Processes in Flagellar Gene Regulation and Biosynthesis in Campylobacter jejuni. J. Bacteriol. 191: 6602-6611 [Abstract] [Full Text]  
  • Blevins, J. S., Xu, H., He, M., Norgard, M. V., Reitzer, L., Yang, X. F. (2009). Rrp2, a {sigma}54-Dependent Transcriptional Activator of Borrelia burgdorferi, Activates rpoS in an Enhancer-Independent Manner. J. Bacteriol. 191: 2902-2905 [Abstract] [Full Text]  
  • Joslin, S. N., Hendrixson, D. R. (2009). Activation of the Campylobacter jejuni FlgSR Two-Component System Is Linked to the Flagellar Export Apparatus. J. Bacteriol. 191: 2656-2667 [Abstract] [Full Text]  


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