Studies on lipase directed export of Escherichia coli β-lactamase in Staphylococcus carnosus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-07

AUTHORS

Wolfgang Liebl, Friedrich Götz

ABSTRACT

The lipase (lip) gene of Staphylococcus hyicus was used to study the expression of the Escherichia coli β-lactamase (bla) gene in S. carnosus. The bla gene, devoid of its promotor and most of the signal sequence, was fused to the lip structural gene at various positions. A set of 11 secretion vectors (pLLβ1 to pLLβ11) was isolated and analysed. All secretion vectors caused β-lactamase production and activity in S. carnosus. However, the amount of hybrid proteins secreted was influenced by the length of the NH2-terminal lipase portion. An increased concentration, comparable to that of the native lipase, of secreted lipase/β-lactamase hybrid proteins was only found when the lipase portion of the construct comprised more than 101 amino acids of the NH2-terminal region of the lipase preprotein; the proposed lipase signal peptide is 36 amino acids long. If the hybrid proteins constructed contained 101 or less amino acids of the NH2-terminal lipase preprotein, only low amounts of secreted hybrid proteins were detectable and a significant portion of the hybrid proteins and β-lactamase activity was found in the cellular fraction. The results indicate that the lipase possesses adjacent to the signal peptide a peptide domain that is essential for the secretion of the lipase/β-lactamase hybrid proteins. More... »

PAGES

166-173

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00330205

DOI

http://dx.doi.org/10.1007/bf00330205

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014766584

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3018441


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