| Literature DB >> 3137209 |
H Lichenstein1, M E Brawner, L M Miles, C A Meyers, P R Young, P L Simon, T Eckhardt.
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.Entities:
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Year: 1988 PMID: 3137209 PMCID: PMC211391 DOI: 10.1128/jb.170.9.3924-3929.1988
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490