Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins.
The major outer membrane lipoprotein (Lpp) of Escherichia coli is released from the cytoplasmic membrane into the periplasm as a complex with LolA, a periplasmic chaperone, prior to the localization in the outer membrane. To determine whether or not LolA is generally involved in the outer membrane localization of lipoproteins in vivo, the chromosomal lolA gene was manipulated so as to be controlled by the lac promoter-operator. Depletion of LolA caused a severe growth defect, and impaired the outer membrane localization of Lpp and Pal, another outer membrane lipoprotein. Although LolA depletion did not immediately arrest the growth of cells lacking Lpp, disruption of the chromosomal lolA gene was lethal to the lpp strain, indicating that LolA is generally required for the outer membrane localization of lipoproteins, and therefore essential irrespective of the presence or absence of Lpp.
Tajima
T
T
Institute of Molecular and Cellular Biosciences, The University of Tokyo, Japan.
Yokota
N
N
Matsuyama
S
S
Tokuda
H
H
D001426:Bacterial Proteins / Q000235:genetics*; D002455:Cell Division; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D017353:Gene Deletion; D008074:Lipoproteins / Q000235:genetics* / Q000502:physiology; D018832:Molecular Chaperones / Q000235:genetics*; D033902:Periplasmic Binding Proteins
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008074:Lipoproteins; C116111:LolA protein, E coli; D018832:Molecular Chaperones; D033902:Periplasmic Binding Proteins