期刊
JOURNAL OF BACTERIOLOGY
卷 186, 期 9, 页码 2692-2698出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.9.2692-2698.2004
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资金
- NIGMS NIH HHS [R15 GM067668, 1R15 GM 67668-01] Funding Source: Medline
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.
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