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Biophys J, December 2002, p. 3152-3161, Vol. 83, No. 6

The Motion of a Single Molecule, the lambda -Receptor, in the Bacterial Outer Membrane

Lene Oddershede,* Jakob Kisbye Dreyer,* Sonia Grego, Stanley Brown,dagger and Kirstine Berg-Sørensen*Dagger

 *The Niels Bohr Institute, University of Copenhagen, 2100 Copenhagen Ø, Denmark;  dagger Department of Molecular, Cell Biology, University of Copenhagen, Øster Farigmagsgade 2A, 1353 Copenhagen K, Denmark; and  Dagger NORDITA, 2100 Copenhagen Ø, Denmark

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 sime  25 nm, the receptor diffuses with a diffusion constant of (1.5 ± 1.0) × 10-9 cm2/s and sits in a harmonic potential as if it were tethered by an elastic spring of spring constant of ~1.0 × 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.

Biophys J, December 2002, p. 3152-3161, Vol. 83, No. 6
© 2002 by the Biophysical Society   0006-3495/02/12/3152/10  $2.00


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