Emulating membrane protein evolution by rational design.

Mikaela Rapp, Susanna Seppälä, Erik Granseth, Gunnar von Heijne

Journal: Science (New York, N.Y.) 2007;315(5816):1282-4

PMID: 17255477

Abstract

How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-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 occurrence of membrane proteins with an internal pseudo-two-fold symmetry axis in the plane of the membrane.

Address: Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

DOI: 10.1126/science.1135406

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MeSH Terms: Amino Acid Sequence, Antiporters, Cell Membrane, Dimerization, Directed Molecular Evolution, Drug Resistance, Bacterial, Escherichia coli, Escherichia coli Proteins, Ethidium, Evolution, Molecular, Gene Duplication, Membrane Transport Proteins, Molecular Sequence Data, Mutation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Recombinant Fusion Proteins