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. 1996 Nov;46(4):347-52.

Native and heterologous protein secretion by Streptomyces lividans

M Sathyamoorthy  1 , D Stemke, M K Speedie
Affiliations
  • PMID: 8987722

Native and heterologous protein secretion by Streptomyces lividans

M Sathyamoorthy et al. Appl Microbiol Biotechnol. 1996 Nov.

Abstract

The secretion of the heterologous parathion phosphotriesterase in S. lividans using the Streptomyces beta-galactosidase signal sequence was further characterised using a pulse/chase system. Unsecreted cell-associated protein in both the precursor and signal-cleaved forms was observed when the protein was expressed from both low- and high-copy vectors. Fractionation of the cells followed by immunoprecipitation with phosphotriesterase antibody suggests that the precursor is membrane-bound while the signal cleaved form is present in the soluble fraction. Preliminary data on the processing of alpha-amylase, a native streptomyces protein, showed much more rapid processing and secretion, but nevertheless still revealed cell-associated, signal-cleaved protein.

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