PMID: 7538961Apr 1, 1995Paper

Channel-forming properties and structural homology of major outer membrane proteins from Pseudomonas fluorescens MFO and OE 28.3

FEMS Microbiology Letters
E DéG Molle

Abstract

The major outer membrane proteins (OprF) from Pseudomonas fluorescens MFO and OE 28.3 were purified by a new method involving native electrophoresis in octyl-polyoxyethylene media. Both proteins, characterized by the same size, heat-modifiability and N-terminal sequence were re-incorporated in virtually solvent-free planar lipid bilayers. They displayed very similar channel-forming properties: the major conductance level was between 250 pS and 270 pS in 1 M NaCl. From experiments of zero-current potential, both porins were determined weakly cation selective. Amplification by PCR and sequencing of the oprF gene of strain MFO allowed to point out 94% identity between the amino acid sequences of these two OprFs isolated from ecological niches as different as milk (strain MFO) and soil (strain OE 28.3).

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Citations

May 29, 2012·Journal of Bacteriology·Etsuko Sugawara, Hiroshi Nikaido
Aug 18, 2006·Environmental Microbiology·Josselin BodilisSylvie Barray
Mar 22, 2006·Microbiology·Josselin Bodilis, Sylvie Barray
Jun 17, 2006·Biochemical and Biophysical Research Communications·Thomas JaouenEmmanuelle Dé

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