Structural and functional characterization of the lexA gene of Xanthomonas campestris pathovar citri.
Mol Genet Genomics
; 265(2): 316-26, 2001 Apr.
Article
en En
| MEDLINE
| ID: mdl-11361343
The role of the LexA protein and, specifically, its effect on recA expression were analyzed in Xanthomonas campestris pathovar citri (X.c. pv. citri). Overexpression of LexA from X.c. pv. citri, in the plant pathogen, as well as in Escherichia coli, results in increased sensitivity to the DNA-damaging agents mitomycin C and ultraviolet radiation, indicating that the recombinant X.c. pv. citri LexA protein is functional in a different bacterial species. Immunoblot analysis revealed that the overexpressed LexA protein functioned as a repressor of recA expression in X.c. pv. citri, and that the mitomycin C-induced increase in the abundance of RecA was accompanied by specific proteolysis of LexA that required RecA. Although the LexA protein from X.c. pv. citri also blocked the expression of recA in E. coli, the E. coli RecA protein was not able to support the autocatalytic cleavage of LexA from the plant pathogen. The transcription start site of the X.c. pv. citri lexA gene was identified, and the region upstream of this gene was shown to confer responsiveness to mitomycin C on a luciferase reporter gene construct. Electrophoretic mobility-shift assays demonstrated that X.c. pv. citri LexA interacts with the promoter region of X.c. pv. citri lexA, as well as with those of the recA genes of X.c. pv. citri and E. coli. These results indicate that LexA functions as a repressor of gene expression in X.c. pv. citri just as it does in E. coli.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Rec A Recombinasas
/
Proteínas Represoras
/
Proteínas Bacterianas
/
Serina Endopeptidasas
/
Regulación Bacteriana de la Expresión Génica
/
Xanthomonas campestris
/
Proteínas de Unión al ADN
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Mol Genet Genomics
Asunto de la revista:
BIOLOGIA MOLECULAR
/
GENETICA
Año:
2001
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Alemania