Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE.
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.
Miyamoto
Atsuki
A
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Japan.
Matsuyama
Shin-ichi
S
Tokuda
Hajime
H
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D010641:Phenotype; D017354:Point Mutation; D011510:Proteolipids / Q000378:metabolism
D018528:ATP-Binding Cassette Transporters; D029968:Escherichia coli Proteins; C407982:LolC protein, E coli; C407983:LolD protein, E coli; C407984:LolE protein, E coli; D018832:Molecular Chaperones; D011510:Proteolipids; C020485:proteoliposomes