Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance.
Lipoproteins of Escherichia coli are sorted to the outer membrane through a pathway composed of five Lol proteins. LolA transports lipoproteins released from the inner membrane by LolCDE to LolB on the outer membrane via the periplasm. Interaction between LolA and LolB was speculated to be strong when LolA binds lipoprotein. However, due to a lack of a sensitive method, the kinetics of this reaction have not been examined in detail. We report here the detection of lipoprotein transfer in real time by means of surface plasmon resonance. The kinetic parameters of lipoprotein transfer were determined with wild-type LolA and a mutant defective in it.
Tsukahara
Jun
J
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
Narita
Shin-Ichiro
S
Tokuda
Hajime
H
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D007700:Kinetics; D008074:Lipoproteins / Q000378:metabolism*; D018832:Molecular Chaperones; D033902:Periplasmic Binding Proteins / Q000378:metabolism*; D011485:Protein Binding; D020349:Surface Plasmon Resonance / Q000379:methods*
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008074:Lipoproteins; C116111:LolA protein, E coli; C087012:LolB protein, E coli; D018832:Molecular Chaperones; D033902:Periplasmic Binding Proteins