Coordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene.
J Bacteriol
; 175(9): 2589-98, 1993 May.
Article
en En
| MEDLINE
| ID: mdl-8478325
ABSTRACT
A 5.9-kb DNA fragment was cloned from Pseudomonas aeruginosa PA103 by its ability to functionally complement a fur mutation in Escherichia coli. A fur null mutant E. coli strain that contains multiple copies of the 5.9-kb DNA fragment produces a 15-kDa protein which cross-reacts with a polyclonal anti-E. coli Fur serum. Sequencing of a subclone of the 5.9-kb DNA fragment identified an open reading frame predicted to encode a protein 53% identical to E. coli Fur and 49% identical to Vibrio cholerae Fur and Yersinia pestis Fur. While there is extensive homology among these Fur proteins, Fur from P. aeruginosa differs markedly at its carboxy terminus from all of the other Fur proteins. It has been proposed that this region is a metal-binding domain in E. coli Fur. A positive selection procedure involving the isolation of manganese-resistant mutants was used to isolate mutants of strain PA103 that produce altered Fur proteins. These manganese-resistant Fur mutants constitutively produce siderophores and exotoxin A when grown in concentrations of iron that normally repress their production. A multicopy plasmid carrying the P. aeruginosa fur gene restores manganese susceptibility and wild-type regulation of exotoxin A and siderophore production in these Fur mutants.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Oligopéptidos
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Pseudomonas aeruginosa
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Proteínas Represoras
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Proteínas Bacterianas
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Toxinas Bacterianas
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ADP Ribosa Transferasas
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Sideróforos
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Factores de Virulencia
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Exotoxinas
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Genes Bacterianos
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
1993
Tipo del documento:
Article