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J. Biol. Chem., Vol. 278, Issue 11, 9092-9099, March 14, 2003
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From the We have studied the folding pathway of a
Folding and Insertion of the Outer Membrane Protein OmpA Is
Assisted by the Chaperone Skp and by Lipopolysaccharide*
,
Fachbereich Biologie, Fach M 694, Universität Konstanz, D-78457 Konstanz, Germany, the
§ Abteilung Molekulare Genetik und Präparative
Molekularbiologie, Institut für Mikrobiologie und Genetik, Georg
August Universität Göttingen, Grisebachstrasse 8, D-37077
Göttingen, Germany, and the ¶ Strukturbiochemie,
Forschungszentrum Borstel, Parkallee 22, D-23845 Borstel, Germany
-barrel membrane protein using outer membrane protein A (OmpA) of
Escherichia coli as an example. The deletion of the gene of
periplasmic Skp impairs the assembly of outer membrane proteins of
bacteria. We investigated how Skp facilitates the insertion and folding
of completely unfolded OmpA into phospholipid membranes and which are
the biochemical and biophysical requirements of a possible Skp-assisted
folding pathway. In refolding experiments, Skp alone was not sufficient to facilitate membrane insertion and folding of OmpA. In addition, lipopolysaccharide (LPS) was required. OmpA remained unfolded when
bound to Skp and LPS in solution. From this complex, OmpA folded
spontaneously into lipid bilayers as determined by electrophoretic mobility measurements, fluorescence spectroscopy, and circular dichroism spectroscopy. The folding of OmpA into lipid bilayers was
inhibited when one of the periplasmic components, either Skp or LPS,
was absent. Membrane insertion and folding of OmpA was most efficient
at specific molar ratios of OmpA, Skp, and LPS. Unfolded OmpA in
complex with Skp and LPS folded faster into phospholipid bilayers than
urea-unfolded OmpA. Together, these results describe a first assisted
folding pathway of an integral membrane protein on the example of
OmpA.
*
This work was supported by Grants KL 1024/2-2 and KL
1024/2-3 from the Deutsche Forschungsgemeinschaft (to J. H. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
49-7531-88-3360; Fax: 49-7531-88-3183; E-mail:
joerg.helmut.kleinschmidt@ uni-konstanz.de.
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