| Summary: | 碩士 === 國立交通大學 === 生物科技研究所 === 85 === abstract Thioredoxin
appears to play a variety of roles in different cell types. It
was isolated initially as a co-factor for the reduction of
ribonucleotide diphosphatesby ribonucleotide reductase, has
recently been shown to be required for the assemblyof the
filamentous Escherichia coli phages f1, fd, M13, and required
for phage T7growth. T7 DNA polymerase is composed of the gene
5 protein of the phage and Thioredoxin. Interaction has been
predicted as an engine for phage assembly between the geneI
protein of filamentous phage and thioredoxin system. However,
little is known of of the role of thioredoxin in different"
protein-protein interaction" types. In order to understand the
influence of the different amino acid substitutionsin E.coli
thioredoxin on the growth of bacteriophages T7 and filamentous
phages , we have constructed a mutant in the thioredoxin gene
changing its catalytic core.PCR site-directed-mutagenesis was
crrried out to replace conservative Gly33 by Asp. The mutant was
characterized using an in vivo assay based on the ability of
cellto support growth of T7 and filamentous phages. The results
indicated that the charged group side-chain in the position 33
of amino acid residues have great effecton the growth of
filamentous phages, and little effect on the growth of T7
phages.
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