PMID:12496085
| Citation |
Oddershede, L, Dreyer, JK, Grego, S, Brown, S and Berg-Sørensen, K (2002) The motion of a single molecule, the lambda-receptor, in the bacterial outer membrane. Biophys. J. 83:3152-61 |
|---|---|
| Abstract |
Using optical tweezers and single particle tracking, we have revealed the motion of a single protein, the lambda-receptor, in the outer membrane of living Escherichia coli bacteria. We genetically modified the lambda-receptor placing a biotin on an extracellular site of the receptor in vivo. The efficiency of this in vivo biotinylation is very low, thus enabling the attachment of a streptavidin-coated bead binding specifically to a single biotinylated lambda-receptor. The bead was used as a handle for the optical tweezers and as a marker for the single particle tracking routine. We propose a model that allows extraction of the motion of the protein from measurements of the mobility of the bead-molecule complex; these results are equally applicable to analyze bead-protein complexes in other membrane systems. Within a domain of radius approximately 25 nm, the receptor diffuses with a diffusion constant of (1.5 +/- 1.0) x 10(-9) cm(2)/s and sits in a harmonic potential as if it were tethered by an elastic spring of spring constant of ~1.0 x 10(-2) pN/nm to the bacterial membrane. The purpose of the protein motion might be to facilitate transport of maltodextrins through the outer bacterial membrane. |
| Links |
PubMed PMC1302393 Online version:10.1016/S0006-3495(02)75318-6 |
| Keywords |
Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/physiology; Biotin/chemistry; Biotin/genetics; Biotinylation/methods; Computer Simulation; Elasticity; Escherichia coli/chemistry; Escherichia coli/physiology; Escherichia coli/ultrastructure; Lasers; Micromanipulation/instrumentation; Micromanipulation/methods; Microspheres; Models, Biological; Models, Chemical; Motion; Nanotechnology/instrumentation; Nanotechnology/methods; Optics and Photonics/instrumentation; Particle Size; Porins; Protein Conformation; Receptors, Virus/chemistry; Receptors, Virus/genetics; Receptors, Virus/physiology; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Streptavidin/chemistry; Stress, Mechanical |
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