The dimerization equilibrium of a ClC Cl(-)/H(+) antiporter in lipid bilayers.

Abstract:

:Interactions between membrane protein interfaces in lipid bilayers play an important role in membrane protein folding but quantification of the strength of these interactions has been challenging. Studying dimerization of ClC-type transporters offers a new approach to the problem, as individual subunits adopt a stable and functionally verifiable fold that constrains the system to two states - monomer or dimer. Here, we use single-molecule photobleaching analysis to measure the probability of ClC-ec1 subunit capture into liposomes during extrusion of large, multilamellar membranes. The capture statistics describe a monomer to dimer transition that is dependent on the subunit/lipid mole fraction density and follows an equilibrium dimerization isotherm. This allows for the measurement of the free energy of ClC-ec1 dimerization in lipid bilayers, revealing that it is one of the strongest membrane protein complexes measured so far, and introduces it as new type of dimerization model to investigate the physical forces that drive membrane protein association in membranes.

journal_name

Elife

journal_title

eLife

authors

Chadda R,Krishnamani V,Mersch K,Wong J,Brimberry M,Chadda A,Kolmakova-Partensky L,Friedman LJ,Gelles J,Robertson JL

doi

10.7554/eLife.17438

subject

Has Abstract

pub_date

2016-08-03 00:00:00

issn

2050-084X

journal_volume

5

pub_type

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