NDLI: Secretion of the Escherichia coli outer membrane proteins OmpA and OmpF in Bacillus subtilis is blocked at an early intracellular step

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Secretion of the Escherichia coli outer membrane proteins OmpA and OmpF in Bacillus subtilis is blocked at an early intracellular step

Content Provider	Scilit
Author	Puohiniemi, Ritvaleena Simonen, Marjo Muttilainen, Susanna Himanen, Juha-Pekka Sarvas, Matti
Copyright Year	1992
Description	Journal: Molecular microbiology When the genes coding for the outer membrane (OM) proteins OmpA and OmpF of Escherichia coli are fused to a signal sequence of a bacillar exoenzyme and expressed in Bacillus subtilis they remain cell-bound and the signal sequence is not cleaved. To identify the step of arrest in the export of these proteins we studied their accessibility to protease applied to intact protoplasts; they remained resistant indicating fully intracellular localization. Both proteins appeared associated with the cell membranes in sedimentation and flotation centrifugation experiments. However, OmpA and OmpF proteins synthesized in B. subtilis without a signal sequence were similarly associated with membranes in centrifugation experiments whereas electron microscopy showed the presence of intracytoplasmic inclusion bodies not obviously attached to the cytoplasmic membrane. We conclude that OmpA and OmpF proteins even when provided with a functional signal sequence do not enter the export pathway in B. subtilis, probably owing to lack of a specific export component in B. subtilis.
Ending Page	990
Starting Page	981
ISSN	2573508X
e-ISSN	13652958
DOI	10.1111/j.1365-2958.1992.tb02164.x
Journal	Molecular microbiology
Issue Number	8
Volume Number	6
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1992-04-01
Access Restriction	Open
Subject Keyword	Journal: Molecular microbiology Biochemistry and Molecular Biology Biotechnology and Microbiology
Content Type	Text
Resource Type	Article

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