Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
FEMS microbiology letters
48 (1987), S. 0
ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract Plasmid pBR322 and penP-encoded β-lactamase activities were examined in cell fractions from wild-type and murein lipoprotein-deficient Escherichia coli strains. The specific activity of the Bacillus licheniformis penP gene product, a lipoprotein when expressed in E. coli, was increased in the outer membrane of a murein-lipoprotein deficient mutant. The activities of the 2 enzymes in wild-type E. coli exposed to the translational inhibitor puromycin were also investigated. Synthesis of penP was more susceptible to inhibition by puromycin than the pBR322-encoded TEM1 β-lactamase. The implications of these results for mechanisms of secretion and insertion of lipoproteins into the E. coli outer membrane are discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1987.tb02517.x
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