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. 1987 Aug;169(8):3778-84.
doi: 10.1128/jb.169.8.3778-3784.1987.

Characterization and structure of genes for proteases A and B from Streptomyces griseus

G Henderson, P Krygsman, C J Liu, C C Davey, L T Malek

Characterization and structure of genes for proteases A and B from Streptomyces griseus

G Henderson et al. J Bacteriol. 1987 Aug.

Abstract

Protease A and protease B are extracellular proteins which are secreted by Streptomyces griseus. The genes encoding protease A (sprA) and protease B (sprB) were isolated from an S. griseus genomic library by using a synthetic oligonucleotide probe. Fragments containing sprA and sprB were characterized by hybridization and demonstration of proteolytic activity in Streptomyces lividans. Each DNA sequence contains a large open reading frame with the coding region of the mature protease situated at its carboxy terminus. The amino terminus of each reading frame appears to encode a 38-amino-acid signal peptide followed by a 76- or 78-amino-acid polypeptide, a propeptide, which is joined to the mature protease. Strong homology between the coding regions of the protease genes suggests that sprA and sprB originated by gene duplication.

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References

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