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PubMed1993

Secretion of streptavidin from Bacillus subtilis.

Streptavidin is an extracellular tetrameric protein produced by Streptomyces avidinii. A series of hybrid gene fusions consisting of Bacillus signal peptide coding regions fused to the mature streptavidin sequence were constructed. B. subtilis strains harboring these plasmids accumulate a tetrameric streptavidin in the growth medium. The properties of the streptavidin produced by B. subtilis are similar to those of the streptavidin produced by S. avidinii. B. subtilis strains carrying the various fusions can be grown to a high cell density in a biotin-free medium. Thus, B. subtilis represents an alternate host system for the production of streptavidin.

Amino Acid Sequence↗

PubMed1992

Modular expression and secretion vectors for Bacillus subtilis.

A modular vector system has been developed for the extracellular production of heterologous proteins in Bacillus subtilis. This modular vector system consists of four secretion vectors which are based upon the genes encoding the Bacillus amyloliquefaciens extracellular alkaline protease, neutral protease, barnase and levansucrase. The modular vectors contain compatible restriction sites downstream from the signal peptide-coding region. Three reporter proteins (staphylococcal protein A, levansucrase and Escherichia coli alkaline phosphatase) that offer complementary advantages for cloning, genetic manipulations and media optimization have been fused to the various signal peptides. These secretion vectors function in E. coli and hence can be used to compare the mechanisms of protein secretion in E. coli and B. subtilis.

Alkaline Phosphatase↗