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 Bacterioljournal_title
Journal of bacteriologyauthors
Smith JA,Magnuson RDdoi
10.1128/jb.186.9.2692-2698.2004keywords:
subject
Has Abstractpub_date
2004-05-01 00:00:00pages
2692-8issue
9eissn
0021-9193issn
1098-5530journal_volume
186pub_type
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更新日期:1980-02-01 00:00:00
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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更新日期:1996-01-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:1996-10-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1996-09-01 00:00:00
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更新日期:2007-04-01 00:00:00
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pub_type: 杂志文章
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更新日期:2004-05-01 00:00:00