Modular organization of the Phd repressor/antitoxin protein.

Abstract:

: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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Smith JA,Magnuson RD

doi

10.1128/jb.186.9.2692-2698.2004

keywords:

subject

Has Abstract

pub_date

2004-05-01 00:00:00

pages

2692-8

issue

9

eissn

0021-9193

issn

1098-5530

journal_volume

186

pub_type

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