Characterization of tryptophan synthetase produced in E. coli from the cloned yeast (Saccharomyces cerevisiae) TRP5 gene = 대장균에서 발현된 효모 tryptophan synthetase의 생화학 및 면역학적 성질에 대한 연구

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Title
Characterization of tryptophan synthetase produced in E. coli from the cloned yeast (Saccharomyces cerevisiae) TRP5 gene = 대장균에서 발현된 효모 tryptophan synthetase의 생화학 및 면역학적 성질에 대한 연구
Author(s)
Hyang Sook Yoo; J A Carbon
Bibliographic Citation
Korean Biochemical Journal, vol. 24, no. 2, pp. 127-140
Publication Year
1991
Abstract
The yeast tryptophan synthetase gene (TRP5) cloned in E. coli is functionally expressed and can complement trpAB deletion mutation in E. coli. We have partially purified the tryptophan synthetase from the yeast, Saccharomyces cerevisiae and trpAB, deleted E. coli containing the yeast recombinant plasmid pYe(/^5)2-ll and examined their biochemical and immunological characteristics. Sephadex G-200 gel filtration of the partially purified enzymes show that the molecular weight of the enzyme produced in E. coli by the pYe(於夕5)2-11 is nearly the same (160,000) as that of authentic yeast tryptophan synthetase (155,000). SDS-acrylamide gel analysis of the proteins produced from the E. coli minicells containing yeast TRP5 recombinant plasmid show that the subunit size of yeast tryptophan synthetase produced in E. coli is 72,500, approximately same as the subunit from the native yeast enzyme. Antibody raised against partially purified yeast tryptophan synthetase inactivates the enzyme activity produced in trpAB deleted E. coli by the yeast recombinant plasmids pYe(於가 5). This indicates that tryptophan synthetase produced from the yeast TRP5 gene cloned in E. coli is very similar or identical to the native yeast tryptophan synthetase in its biochemical and immunological characteristics and is different from E. coli tryptophan synthetase. This suggests that large mRNAs must be synthesized from the eucaryotic DNA by the E. coli RNA polymerase and the yeast translational signals are recognized by the E. coli ribosomes, initiation and termination components.
ISSN
0368-4881
Publisher
Korea Soc-Assoc-Inst
Type
Article
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1. Journal Articles > Journal Articles
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