Secretion of interleukin-1 beta and Escherichia coli galactokinase by Streptomyces lividans.
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.
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005686:Galactokinase / Q000378:metabolism*; D007118:Immunoassay; D007375:Interleukin-1 / Q000378:metabolism*; D053583:Interleukin-1beta; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D010957:Plasmids; D021382:Protein Sorting Signals / Q000235:genetics / Q000502:physiology; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D001616:beta-Galactosidase / Q000235:genetics
D007375:Interleukin-1; D053583:Interleukin-1beta; D010446:Peptide Fragments; D021382:Protein Sorting Signals; C052994:interleukin-1beta (163-171); D005686:Galactokinase; D001616:beta-Galactosidase