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Emulating Membrane Protein Evolution by Rational Design
Mikaela Rapp,1*Susanna Seppälä,1*Erik Granseth,1,2Gunnar von Heijne1,2
How do integral membrane proteins evolve in size and complexity?Using the small multidrug-resistance protein EmrE from Escherichiacoli as a model, we experimentally demonstrated that the evolutionof membrane proteins composed of two homologous but oppositelyoriented domains can occur in a small number of steps: An originaldual-topology protein evolves, through a gene-duplication event,to a heterodimer formed by two oppositely oriented monomers.This simple evolutionary pathway can explain the frequent occurrenceof membrane proteins with an internal pseudo–two-foldsymmetry axis in the plane of the membrane.
1 Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden. 2 Stockholm Bioinformatics Center, AlbaNova, SE-106 91 Stockholm, Sweden.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: gunnar{at}dbb.su.se
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