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J Bacteriol, February 1998, p. 909-913, Vol. 180, No. 4
Laboratoire d'Ecologie Microbienne de la
Rhizosphère,
Received 28 July 1997/Accepted 16 December 1997
A 38-kDa major outer membrane protein (OMP) was isolated from the
nitrogen-fixing enterobacterium Rahnella aquatilis CF3. This protein exists as a stable trimer in the presence of 2% sodium dodecyl sulfate at temperatures below 60°C. Single channel
experiments showed that this major OMP of R. aquatilis CF3
is able to form pores in the planar lipid membrane. Two
oligonucleotides encoding the N-terminal portion of the 38-kDa OMP and
C-terminal portion of OmpC were used to amplify the 38-kDa gene by PCR.
The deduced amino acid sequence showed a strong homology with
Escherichia coli, Klebsiella pneumoniae,
Salmonella typhi, and Serratia marcescens OmpC
sequences, except loops L6 and L7, which are postulated to be cell
surface exposed. On the basis of the OmpF-PhoE
three-dimensional structure, it seems likely that this 38-kDa organizes
three 16-strand
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Major Outer Membrane Protein of Rahnella aquatilis
Functions as a Porin and Root Adhesin
-barrel subunits. The relationship between the
structure and the double functionality of this protein as porin and as
a root adhesin is discussed.
*
Corresponding author. Mailing address: Laboratoire
d'Ecologie Microbienne de la Rhizosphère, DSV-DEVM, UMR 163 CNRS-CEA, CEA Cadarache, F-13108 Saint Paul lez Durance, France. Phone: (33) 44225 4961. Fax: (33) 44225 6648. E-mail:
achouak{at}soumman.cad.cea.fr.
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