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Influence of the different amino acid substitutions in Escherichia coli thioredoxin on the growth of bacteriophages T7 and f1
Author(s) -
Minárik Peter,
Kollárová Marta,
Brunovská Alena
Publication year - 1993
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620330314
Subject(s) - escherichia coli , chemistry , microbiology and biotechnology , thioredoxin , amino acid , bacteriophage , biochemistry , biology , gene
We have constructed three mutants in the thioredoxin ( trx A) 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 trx A 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.