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Expression of the carboxypeptidase T gene from Thermoactinomyces vulgaris in stable protoplast type L-forms of Proteus mirabilis. 1998
A M Bushueva, and
A B Shevelev, and
J Gumpert, and
G G Chestukhina, and
A V Serkina, and
C Hoischen, and
M V Matz, and
M V Kuryatova, and
V M Stepanov
Laboratory of Protein Chemistry, Institute of Microbial Genetics (GNII Genetika), Moscow, Russia.
The structural gene of the carboxypeptidase T (cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l-1 and should be improvable.
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