SUMMARY: A SDS-resistant, Ca-dependent serine exoprotease gene, cloned on a 7-1 kb DNA fragment in the recombinant plasmid pVP100, was expressed from its own promoter in . Although active exoprotease was produced by late stationary phase (pVP100) cultures after 15 h incubation in proteinaceous medium containing Ca, transcription and translation of the exoprotease occurred before 6 h, during exponential growth. The cloned exoprotease was synthesized as a pool of inactive precursor molecules during exponential growth, and released as active exoprotease 8 h later by a process which did not require protein synthesis or involve cell lysis. Release of the exoprotease by (pVP100) was not inhibited by -phenanthroline, quinacrine or cerulenin. Supernatant samples from (pVP100) cultures contained two SDS-resistant exoproteases with apparent values of approximately 54000 and 39000. The cloned exoprotease activity was inhibited by EDTA and a serine protease inhibitor, but was not affected by an inhibitor of trypsin-like enzymes.


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