PMID:12297303

Citation	Miyamoto, A, Matsuyama, S and Tokuda, H (2002) Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE. FEBS Lett. 528:193-6
Abstract	Periplasmic molecular chaperone LolA and the inner membrane ATP binding cassette transporter LolCDE are essential for ATP-dependent release of outer membrane-directed lipoproteins from the inner membrane of Escherichia coli. A LolA(F47E) mutant carrying a Phe to Glu mutation at position 47 was defective in the release of lipoproteins from spheroplasts and proteoliposomes reconstituted with LolCDE. When incubated with proteoliposomes containing LolCDE, LolA remained in the supernatant whereas LolA(F47E) bound to proteoliposomes. This tight association of LolA(F47E) with LolCDE caused a dominant negative phenotype in vivo, suggesting that the LolA-LolCDE interaction is critical for lipoprotein release.
Links	PubMed
Keywords	ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Phenotype; Point Mutation; Proteolipids/metabolism
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