Abstract
A heterologous phosphotriesterase (parathion hydrolase) was previosly shown to be secreted by Streptomyces lividans. To investigate the mechanism of secretion, a system to label the protein and follow its expression and secretion was developed. The recombinant S. lividans was grown first in a defined medium containing [35S]methionine that permitted expression but not secretion. It was then transferred to tryptone/glucose medium with unlabeled methionine for the chase period, during which secretion was observed. The results indicate a relatively slow rate of secretion that is also dependent on the growth medium.
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Sathyamoorthy, M., Speedie, M.K. Monitoring transport of a recombinant phosphotriesterase in Streptomyces lividans using a pulse-chase system. Appl Microbiol Biotechnol 43, 493–497 (1995). https://doi.org/10.1007/BF00218455
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DOI: https://doi.org/10.1007/BF00218455