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Construction of an escherichia coli initiation mutant thioredoxin gene by site directed mutagenesis an alternative translational initiation for escherichia coli trxa gene



Construction of an escherichia coli initiation mutant thioredoxin gene by site directed mutagenesis an alternative translational initiation for escherichia coli trxa gene



Korean Biochemical Journal 24(5): 488-496



The mRNA produced from the E. coli thioredoxin gene (trxA) contains two potential translational initiation sites, one of which could initiate the synthesis of a protein 19 amino acids longer than the E. coli well-known thioredoxin of 108 amino acid residues. However, the expression of extended thioredoxin was not yet confirmed. To dissect translations from two initiation codons, the second ATG codon was converted to CTG by site-directed mutagenesis. The initiation-mutant thioredoxin gene lacking the second ATG codon could produce only the extended thioredoxin, which prove another translational initiation from the first ATG codon of an E. coli trxA mRNA. In vivo characteristics of the extended thioredoxin were examined in the several aspects. Just like the well-known thioredoxin, the extended thioredoxin is able to serve as a subunit of T7 DNA polymerase. In contrast, it doesn't act as a cofactor for methionine sulfoxide reductase.

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Accession: 007154747

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