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J Biol Chem, Vol. 274, Issue 8, 5114-5119, February 19, 1999
,
From the Lipopolysaccharides (LPS) are amphiphilic
molecules in the outer leaflet of the bacterial outer membrane.
Recently, an early role for LPS in the folding of outer membrane porin
PhoE was demonstrated in vitro. In order to elucidate the
molecular mechanism of LPS-protein interactions, folding of PhoE
protein was studied with a large set of well characterized LPS
chemotypes. We demonstrate that negative charges in the inner core
region contribute to the high efficiency of folding of PhoE protein. In
addition, the supramolecular structure of the LPS aggregate seems to be
important. LPS with a lipid A part that prefers a lamellar or a direct
micellar structure and a high state of order of its acyl chains is much
less efficient to support folding as compared with LPS with lipid A
that prefers a non-lamellar structure and a low acyl chain order. These
in vitro data indicate that extensive interactions between
the core and lipid A region of LPS with the protein are required to
support protein folding. The LPS-PhoE binding might be promoted by the presence of hydroxy fatty acids in the lipid A moiety of LPS.
Department of Molecular Cell Biology,
Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands and ¶ Research Center
Borstel, Departments of Immunochemistry and Biochemical Microbiology,
Parkallee 1-40, D-23845 Borstel, Germany
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