The effect of signal sequences on the efficiency of secretion of a heterologous phosphotriesterase by Streptomyces lividans

Sharon S. Rowland, James J. Zulty, Malathi Sathyamoorthy, Burton M. Pogell, Marilyn K. Speedie

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

A heterologous phosphotriesterase (parathion hydrolase) containing the native Flavobacterium species signal sequence was previously shown to be secreted by Streptomyces lividans. Western blot analysis of the recombinant phosphotriesterase produced by S. lividans demonstrated only the mature form extracellular but both processed and unprocessed forms in cell-associated samples. To investigate the efficiency of secretion in Streptomyces, a construction was made that substituted a native Streptomyces β-galactosidase signal sequence for the Flavobacterium signal sequence. This resulted in a higher proportion of hydrolase in the extracellular fluid and a lower proportion of parathion hydrolase remaining cell-associated. These results suggest that use of a native Streptomyces signal sequence may result in more efficient secretion of heterologous proteins.

Original languageEnglish (US)
Pages (from-to)94-100
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume38
Issue number1
DOIs
StatePublished - Oct 1 1992

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