NUCLEOTIDE-SEQUENCE ANALYSIS AND COMPARISON OF THE LEXA GENES FROM SALMONELLA-TYPHIMURIUM, ERWINIA-CAROTOVORA, PSEUDOMONAS-AERUGINOSA AND PSEUDOMONAS-PUTIDA

被引:42
作者
GARRIGA, X [1 ]
CALERO, S [1 ]
BARBE, J [1 ]
机构
[1] AUTONOMOUS UNIV BARCELONA, DEPT GENET & MICROBIOL, BELLATERRA, E-08193 BARCELONA, SPAIN
来源
MOLECULAR AND GENERAL GENETICS | 1992年 / 236卷 / 01期
关键词
LEXA GENE; SALMONELLA-TYPHIMURIUM; ERWINIA-CAROTOVORA; PSEUDOMONAS-AERUGINOSA; PSEUDOMONAS PUTIDA;
D O I
10.1007/BF00279651
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The complete nucleotide sequences of the lexA genes from Salmonella typhimurium, Erwtinia carotovora, Pseudomonas aeruginosa and Pseudomonas putida were determined; the DNA sequences of the lexA genes from these bacteria were 86%, 76%, 61% and 59% similar, respectively, to the Eseherichia coli K12 gene. The predicted amino acid sequences of the S. typhimurium, E. carotovora and P. putida LexA proteins are 202 residues long whereas that of P. aeruginosa is 204. Two putative LexA repressor binding sites were localized up-stream of each of the heterologous genes, the distance between them being 5 bp in S. typhimurium and E. carotovora, as in the lexA gene of E. coli, and 3 bp in P. putida and P. aeruginosa. The first lexA site present in the lexA operator of all five bacteria is very well conserved. However, the second lexA box is considerably more variable. The Ala-84-Gly-85 bond, at which the LexA repressor of E. coli is cleaved during the induction of the SOS response, is also found in the LexA proteins of S. typhimurium and E. carotovora. Likewise, the amino acids Ser-119 and Lys-156 are present in all of these three LexA repressors. These residues also exist in the LexA proteins of P. putida and P. aeruginosa, but they are displaced by 4 and 6 residues, respectively. Furthermore, the structure and sequence of the DNA-binding domain of the LexA repressor of E. coli are highly conserved in the S. typhimurium, E. carotovora, P. aeruginosa and P. putida LexA proteins.
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页码:125 / 134
页数:10
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