Nucleotide sequence and expression of a cloned Thiobacillus ferrooxidans recA gene in Escherichia coli.
The nucleotide sequence of the recA gene of Thiobacillus ferrooxidans has been determined. No SOS box characteristic of LexA-regulated promoters could be identified in the 196-bp region upstream from the coding region. The cloned T. ferrooxidans recA gene was expressed in Escherichia coli from both the lambda pR and lac promoters. It was not expressed from the 2.2-kb of T. ferrooxidans DNA preceding the gene. The T. ferrooxidans recA gene specifies a protein of 346 amino acids that has 66% and 69% homology to the RecA proteins of E. coli and Pseudomonas aeruginosa, respectively. Most amino acids that have been identified as being of functional importance in the E. coli RecA protein are conserved in the T. ferrooxidans RecA protein. Although some amino acids that have been associated with proteolytic activity have been substituted, the cloned protein has retained protease activity towards the lambda and E. coli LexA repressors.
Ramesar
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RS
Department of Microbiology, University of Cape Town, Rondebosch, South Africa.
Abratt
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Woods
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Rawlings
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DE
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases; D011550:Pseudomonas aeruginosa / Q000235:genetics; D011938:Rec A Recombinases / Q000235:genetics*; D013855:Thiobacillus / Q000235:genetics*
D004269:DNA, Bacterial; D011938:Rec A Recombinases; D010447:Peptide Hydrolases