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. 1988 Sep;170(9):3924–3929. doi: 10.1128/jb.170.9.3924-3929.1988

Secretion of interleukin-1 beta and Escherichia coli galactokinase by Streptomyces lividans.

H Lichenstein 1, M E Brawner 1, L M Miles 1, C A Meyers 1, P R Young 1, P L Simon 1, T Eckhardt 1
PMCID: PMC211391  PMID: 3137209

Abstract

The functionality of the Streptomyces lividans beta-galactosidase signal peptide to direct heterologous protein export was examined. The signal peptide plus eight amino acids of mature protein were sufficient to export not only a naturally exported protein, interleukin-1 beta, but also a naturally occurring cytoplasmic protein, Escherichia coli galactokinase. Interestingly, cells which expressed yet exported galactokinase were phenotypically Gal-. The potential use of the exported galactokinase system for the isolation and characterization of mutations within signal peptides and the export machinery of the host is discussed.

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Selected References

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