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EmrE, the smallest ion-coupled transporter, provides a unique paradigm for structure-function studies

S Schuldiner1, M Lebendiker, H Yerushalmi

  • 1Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel. shimons@leonardo.ls.huji.ac.il

The Journal of Experimental Biology
|January 1, 1997
PubMed
Summary

Escherichia coli EmrE transporter, a hydrophobic protein, removes toxicants for proton exchange. Studies suggest EmrE functions as a homo-oligomer, indicating a dimeric or multimeric structure for its transport activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • EmrE is a multidrug transporter in Escherichia coli.
  • It confers resistance to various toxicants by exchanging them for hydrogen ions.
  • EmrE is a 12 kDa hydrophobic protein purified using organic solvents.

Purpose of the Study:

  • To elucidate the structure and function of the EmrE multidrug transporter.
  • To investigate the transmembrane domains and oligomeric state of EmrE.

Main Methods:

  • Protein purification leveraging organic solvent solubility.
  • Transmission Fourier transform infrared spectroscopy to determine secondary structure.
  • Amide proton H/D exchange to assess residue burial within the membrane.
  • Co-reconstitution experiments with wild-type and mutant EmrE proteins.

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Main Results:

  • Hydrophobicity analysis predicted four transmembrane domains.
  • Infrared spectroscopy indicated high alpha-helical content (78-80%).
  • Amide proton H/D exchange suggested ~80% of residues are membrane-embedded.
  • A substrate-binding domain involving Cys41 and Cys95 was identified.
  • Negative dominance in co-reconstitution experiments indicated homo-oligomerization.

Conclusions:

  • EmrE likely possesses four transmembrane alpha-helices.
  • The protein is predominantly embedded within the lipid bilayer.
  • Negative dominance provides evidence that EmrE functions as a homo-oligomer, possibly a dimer.