The effect of signal sequences on the efficiency of secretion of a heterologous phosphotriesterase by Streptomyces lividans
Autor: | Malathi Sathyamoorthy, Marilyn K. Speedie, Sharon S. Rowland, Burton M. Pogell, James J. Zulty |
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Rok vydání: | 1992 |
Předmět: |
Signal peptide
Recombinant Fusion Proteins Molecular Sequence Data Heterologous Protein Sorting Signals Flavobacterium Applied Microbiology and Biotechnology Streptomyces law.invention Bacterial Proteins law Hydrolase Amino Acid Sequence Base Sequence biology Aryldialkylphosphatase Streptomycetaceae General Medicine beta-Galactosidase biology.organism_classification Molecular biology Phosphoric Monoester Hydrolases Biochemistry Recombinant DNA Actinomycetales Protein Processing Post-Translational Biotechnology |
Zdroj: | Applied Microbiology and Biotechnology. 38 |
ISSN: | 1432-0614 0175-7598 |
DOI: | 10.1007/bf00169426 |
Popis: | 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 extracellularly 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 beta-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. |
Databáze: | OpenAIRE |
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