We have constructed three mutants in the thioredoxin (trxA) gene changing its catalytic core between Cys-32 and Cys-35. Oligonucleotide-directed mutagenesis was carried out to replace conservative Gly-33 or Pro-34 by leucine, lysine, glutamine, phenylalanine or tryptophane. The mutants were characterized using an in vivo assay based on the ability of cell (mutants in the chromosomal trxA gene) to support growth of T7 and filamentous f1 phages. The results indicate that the smaller group side-chain in the position 33 and 34 of amino acid residues are indispensable for the growth of phages.
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