ArticleBiochimica et biophysica acta2014
EmrE dimerization depends on membrane environment.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Multidrug resistance transporter EmrE is only moderately sensitive to lipid composition.Biophysical journal · 2026Article
- Comparative genomics of 'Microbial genomics · 2025Article
- Pseudomonas aeruginosa adapts to octenidine via a combination of efflux and membrane remodelling.Communications biology · 2021Article
- Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021Review
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- Inducing conformational preference of the membrane protein transporter EmrE through conservative mutations.eLife · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 2018Article
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Authors and funding
3 authors.
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Abstract
The small multi-drug resistant (SMR) transporter EmrE functions as a homodimer. Although the small size of EmrE would seem to make it an ideal model system, it can also make it challenging to work with. As a result, a great deal of controversy has surrounded even such basic questions as the oligomeric state. Here we show that the purified protein is a homodimer in isotropic bicelles with a monomer-dimer equilibrium constant (KMD(2D)) of 0.002-0.009mol% for both the substrate-free and substrate-bound states. Thus, the dimer is stabilized in bicelles relative to detergent micelles where the KMD(2D) is only 0.8-0.95mol% (Butler et al. 2004). In dilauroylphosphatidylcholine (DLPC) liposomes KMD(2D) is 0.0005-0.0008mol% based on Förster resonance energy transfer (FRET) measurements, slightly tighter than bicelles. These results emphasize the importance of the lipid membrane in influencing dimer affinity.
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