The effect of signal sequences on the efficiency of secretion of a heterologous phosphotriesterase by Streptomyces lividans.
Appl Microbiol Biotechnol
; 38(1): 94-100, 1992 Oct.
Article
em En
| MEDLINE
| ID: mdl-1369409
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 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.
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Base de dados:
MEDLINE
Assunto principal:
Streptomyces
/
Proteínas de Bactérias
/
Proteínas Recombinantes de Fusão
/
Sinais Direcionadores de Proteínas
/
Monoéster Fosfórico Hidrolases
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article