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Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance |
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| Authors: | Jun Tsukahara |
| Institution: | Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan |
| Abstract: | 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.Structured summaryMINT-7259948: mlolB (uniprotkb:P61320) binds (MI:0407) to pal (uniprotkb:P0A912) by surface plasmon resonance (MI:0107) |
| Keywords: | octylglucoside d-glucopyranoside" target="_blank">n-octyl-β-d-glucopyranoside IPTG d-galactopyranoside" target="_blank">isopropyl-1-thio-β-d-galactopyranoside IM inner membrane OM outer membrane SPR surface plasmon resonance SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis |
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