Divergent evolution of membrane protein topology: The Escherichia coli RnfA and RnfE homologues

AUTOR(ES)

Sääf, Annika

FONTE

The National Academy of Sciences

RESUMO

Although the molecular evolution of protein tertiary structure and enzymatic activity has been studied for decades, little attention has been paid to the evolution of membrane protein topology. Here, we show that two closely related polytopic inner membrane proteins from Escherichia coli have evolved opposite orientations in the membrane, which apparently has been achieved by the selective redistribution of positively charged amino acids between the polar segments flanking the transmembrane stretches. This example of divergent evolution of membrane protein topology suggests that a complete inversion of membrane topology is possible with relatively few mutational changes even for proteins with multiple transmembrane segments.

Documentos Relacionados

• Membrane topology of the Escherichia coli ExbD protein.
• Gene fusion analysis of membrane protein topology: a direct comparison of alkaline phosphatase and beta-lactamase fusions.
• Hepadnavirus Envelope Topology: Insertion of a Loop Region in the Membrane and Role of S in L Protein Translocation
• Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.
• Topology of the lac carrier protein in the membrane of Escherichia coli.