Native and heterologous protein secretion by Streptomyces lividans |
| |
Authors: | M. Sathyamoorthy D. Stemke M. K. Speedie |
| |
Affiliation: | (1) Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, 21201 Baltimore, Maryland, USA;(2) Present address: College of Pharmacy, University of Minnesota, 308 Harvard St, S.E., 55455 Minneapolis, Minnesota, USA |
| |
Abstract: | The secretion of the heterologous parathion phosphotriesterase in S. lividans using the Streptomyces -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 -amylase, a native Streptomyces protein, showed much more rapid processing and secretion, but nevertheless still revealed cell-associated, signal-cleaved protein.National Institutes of Health, Laboratory of Host Defence |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|