title: Native and heterologous protein secretion by Streptomyces lividans.
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.
authors.affiliation: Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore 21201, USA.
authors.forename: M
authors.initials: M
authors.lastname: Sathyamoorthy
authors.forename: D
authors.initials: D
authors.lastname: Stemke
authors.forename: M K
authors.initials: MK
authors.lastname: Speedie
mesh_terms: D000595:Amino Acid Sequence; D043303:Aryldialkylphosphatase; D002462:Cell Membrane / Q000201:enzymology; D004950:Esterases / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals; D011994:Recombinant Proteins / Q000378:metabolism; D017421:Sequence Analysis; D013302:Streptomyces / Q000201:enzymology*; D000516:alpha-Amylases / Q000378:metabolism
chemical_list: D011498:Protein Precursors; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D004950:Esterases; D043303:Aryldialkylphosphatase; D000516:alpha-Amylases