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Journal Articles Eur. Biophys. J. Year : 2015

The E.coli Aquaporin Z interface : a puzzle?


Aquaporins are membrane proteins, that act as water channels in biological membranes. Members of this family form tetrameric, or rarely pentameric, complexes in the lipid bilayer. In order to better understand the folding and multimeric assembly of these proteins, we have constructed a series of destabilized proteins by modifying the interface between monomers in Aquaporin Z from E.coli. We have characterized these mutants to test the effects on the folding of the monomeric unit and their ability to form tetramers. We have also examined the consequences modified structures on the function of the water channel and the dynamics of the protein. Structure and folding has been examined at the level of the protein topology to control the helices insertion in the membrane. These methods indicate that the surface mutations do not detactably modify the structure of the monomeric Aquaporin Z. Assembly into tetramers has been investigated by hydrodynamics methods (Gel filtration or DLS, Fluorescence anisotropy and FCS). These methods suggest that, in some mutants, tetramers are not properly formed and monomeric Aquaporins predominate. Some other mutants are able to tetramerize but contrary to the wild type, the assembly do not resist to SDS denaturation. We report the consequences of these changes in assembly on function and dynamics.
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hal-01458192 , version 1 (06-02-2017)


  • HAL Id : hal-01458192 , version 1


Victoria Schmidt, Pierre Hubert, James N. Sturgis. The E.coli Aquaporin Z interface : a puzzle?. Eur. Biophys. J., 2015, 44, pp.S217. ⟨hal-01458192⟩
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