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Journal of Bacteriology, May 2004, p. 2692-2698, Vol. 186, No. 9
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.9.2692-2698.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Modular Organization of the Phd Repressor/Antitoxin Protein

Jeremy Allen Smith and Roy David Magnuson*

Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, Alabama 35899

Received 22 October 2003/ Accepted 14 January 2004

The P1 plasmid addiction operon is a compact genetic structure consisting of promoter, operator, antitoxin gene (phd), and toxin gene (doc). The 73-amino-acid antitoxin protein, Phd, has two distinct functions: it represses transcription (by binding to its operator) and it prevents host death (by binding and neutralizing the toxin). Here, we show that the N terminus of Phd is required for repressor but not antitoxin activity. Conversely, the C terminus is required for antitoxin but not repressor activity. Only a quarter of the protein, the resolution limit of this analysis, was required for both activities. We suggest that the plasmid addiction operon is a composite of two evolutionarily separable modules, an operator-repressor module and an antitoxin-toxin module. Consideration of similar antitoxin proteins and their surroundings indicates that modular exchange may contribute to antitoxin and operon diversity.

* Corresponding author. Mailing address: WH 258, 301 Sparkman Dr., University of Alabama in Huntsville, Huntsville, AL 35899. Phone: (256) 824-6094. Fax: (256) 824-6305. E-mail: magnusr{at}email.uah.edu.

Journal of Bacteriology, May 2004, p. 2692-2698, Vol. 186, No. 9
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.9.2692-2698.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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