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Journal of Bacteriology, August 2007, p. 5683-5691, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.01807-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Vibrio cholerae Quorum-Sensing Regulatory Protein HapR{triangledown}

Rukman S. De Silva,1 Gabriela Kovacikova,2 Wei Lin,2 Ronald K. Taylor,2 Karen Skorupski,2 and F. Jon Kull1*

Department of Chemistry, Dartmouth College,1 Department of Microbiology and Immunology, Dartmouth Medical School, Hanover, New Hampshire 037552

Received 30 November 2006/ Accepted 14 May 2007

Quorum sensing in Vibrio cholerae involves signaling between two-component sensor protein kinases and the response regulator LuxO to control the expression of the master regulator HapR. HapR, in turn, plays a central role in regulating a number of important processes, such as virulence gene expression and biofilm formation. We have determined the crystal structure of HapR to 2.2-Å resolution. Its structure reveals a dimeric, two-domain molecule with an all-helical structure that is strongly conserved with members of the TetR family of transcriptional regulators. The N-terminal DNA-binding domain contains a helix-turn-helix DNA-binding motif and alteration of certain residues in this domain completely abolishes the ability of HapR to bind to DNA, alleviating repression of both virulence gene expression and biofilm formation. The C-terminal dimerization domain contains a unique solvent accessible tunnel connected to an amphipathic cavity, which by analogy with other TetR regulators, may serve as a binding pocket for an as-yet-unidentified ligand.

* Corresponding author. Mailing address: F6128 Burke Laboratory, Department of Chemistry, Dartmouth College, Hanover, NH 03755. Phone: (603) 646-1552. Fax: (603) 646-3946. E-mail: f.jon.kull{at}dartmouth.edu

{triangledown} Published ahead of print on 25 May 2007.

Journal of Bacteriology, August 2007, p. 5683-5691, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.01807-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Tsou, A. M., Cai, T., Liu, Z., Zhu, J., Kulkarni, R. V. (2009). Regulatory targets of quorum sensing in Vibrio cholerae: evidence for two distinct HapR-binding motifs. Nucleic Acids Res 37: 2747-2756 [Abstract] [Full Text]  
  • Lee, D. H., Jeong, H. S., Jeong, H. G., Kim, K. M., Kim, H., Choi, S. H. (2008). A Consensus Sequence for Binding of SmcR, a Vibrio vulnificus LuxR Homologue, and Genome-wide Identification of the SmcR Regulon. J. Biol. Chem. 283: 23610-23618 [Abstract] [Full Text]  
  • Waters, C. M., Lu, W., Rabinowitz, J. D., Bassler, B. L. (2008). Quorum Sensing Controls Biofilm Formation in Vibrio cholerae through Modulation of Cyclic Di-GMP Levels and Repression of vpsT. J. Bacteriol. 190: 2527-2536 [Abstract] [Full Text]  
  • Svenningsen, S. L., Waters, C. M., Bassler, B. L. (2008). A negative feedback loop involving small RNAs accelerates Vibrio cholerae's transition out of quorum-sensing mode. Genes Dev. 22: 226-238 [Abstract] [Full Text]  


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