Secretion of Escherichia coli beta-lactamase from Bacillus subtilis by the aid of alpha-amylase signal sequence.

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Abstract
A secretion vector system for introducing foreign genes into B. subtilis. Secretion vectors were constructed from the plasmid pUB110 and the promoter and signal sequence region of the .alpha.-amylase gene from B. amyloliquefaciens. Foreign structural genes can be inserted into the various vectors after the signal sequence region of the .alpha.-amylase gene. Demonstrating secretion of a foreign gene product from Bacillus, it is reported that the E. coli .beta.-lactamase gene, devoid of its own signal sequence coding region, can be expressed in B. subtilis by the aid of the secretion vectors so that > 95% of the enzyme activity is secreted to the growth medium. Efficient secretion of .beta.-lactamase (penicillin amido-.beta.-lactamhydrolase, EC 3.5.2.6) is observed if the complete signal sequence coding region of the .alpha.-amylase gene precedes the .beta.-lactamase structural gene. An incomplete .alpha.-amylase signal peptide lacking the 6 carboxy-terminal amino acid residues does not promote secretion of the fused .beta.-lactamase, which remains unprocessed and cell-associated.