Native and heterologous protein secretion by Streptomyces lividans

M. Sathyamoorthy, D. Stemke, Marilyn K Speedie

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The secretion of the heterologous parathion phosphotriesterase in S. lividans using the Streptomyces β-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 α-amylase, a native Streptomyces protein, showed much more rapid processing and secretion, but nevertheless still revealed cell-associated, signal-cleaved protein.

Original languageEnglish (US)
Pages (from-to)347-352
Number of pages6
JournalApplied Microbiology and Biotechnology
Volume46
Issue number4
DOIs
StatePublished - Jan 1 1996

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