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Related Experiment Videos

Emulating membrane protein evolution by rational design.

Mikaela Rapp1, Susanna Seppälä, Erik Granseth

  • 1Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Science (New York, N.Y.)
|January 27, 2007
PubMed
Summary
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Integral membrane proteins evolve via gene duplication. A dual-topology protein model demonstrates a simple pathway to oppositely oriented domains, explaining pseudo-symmetry in membrane proteins.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Integral membrane proteins are crucial for cellular functions.
  • Understanding their evolution, particularly their size and complexity, is a key challenge in molecular biology.
  • The small multidrug-resistance protein EmrE from Escherichia coli serves as a model system.

Purpose of the Study:

  • To investigate the evolutionary pathways of integral membrane proteins.
  • To understand how membrane proteins increase in size and complexity.
  • To elucidate the origin of pseudo-two-fold symmetry in membrane proteins.

Main Methods:

  • Utilized the small multidrug-resistance protein EmrE as a model system.
  • Experimentally demonstrated evolutionary steps.

Related Experiment Videos

  • Focused on gene duplication events and domain orientation.

    • Main Results:

    • Showed that integral membrane proteins with two homologous, oppositely oriented domains can evolve rapidly.
    • Demonstrated a pathway from a dual-topology protein to a heterodimer of oppositely oriented monomers.
    • This pathway involves a single gene duplication event.

    Conclusions:

    • A simple gene duplication event can drive the evolution of complex membrane protein structures.
    • This mechanism explains the common occurrence of internal pseudo-two-fold symmetry in membrane proteins.
    • The study provides insights into the evolutionary strategies of membrane proteins.