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KMID : 0545119910010010022
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Journal of Microbiology and Biotechnology
1991 Volume.1 No. 1 p.22 ~ p.30
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Secretion of Bacillus subtilis Cytidine Deaminase by the Aid of Signal Sequences in Escherichia coli
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Yoon, Soo Ryun
Kim, Sung Il/Lee, Se Young/Song, Bang Ho
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Abstract
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In order to secrete the Bacillus subtilis cytidine deaminase (CDase, cytidine/2´-deoxycytidine deaminase) encoded by the B. subtills cdd gene in E, coli by the aid of signal sequences, the cdd gene was fused in-frame to either amyE or penP signal sequences and the gene expression and CDase localization were examined. For the penP signal sequence::cdd fusion, the cdd gene with 9 amino acids truncated from the 5´-terminus was fused in-frame to the signal sequence, then the cdd^+ colonies were not occurred from the minimal plate by cdd complementation. The result suggests that 9 amino acids on the NH_2-terminal of CDase have an essential function in the enzyme activity. The hybrid protein obtained by fused gene amyE signal sequence::cdd structural gene gave cdd^+ phenotype and about half of the total CDase activity was found to be secreted in the periplasm of E. coli transformant JF611/pSO202. The periplasmic CDase activity of JF611 harboring pSO52 containing the intact cdd gene was considerablely lower than that of the cells harboring pSO202 carrying the hybrid cdd gene. This suggests that the CDase was secreted to the periplasm through the cytoplasmic membrane by the aid of the amyE signal sequence in the E. coli transformant.
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