ArticleProceedings of the National Academy of Sciences of the United States of America2004
In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 134 citations in OpenAlex.
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology.Frontiers in molecular biosciences · 2021Review
- Review
- Few Conserved Amino Acids in the Small Multidrug Resistance Transporter EmrE Influence Drug Polyselectivity.Antimicrobial agents and chemotherapy · 2018Article
- Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy.Nature communications · 2015Article
- Efflux by small multidrug resistance proteins is inhibited by membrane-interactive helix-stapled peptides.The Journal of biological chemistry · 2015Article
- EmrE dimerization depends on membrane environment.Biochimica et biophysica acta · 2014Article
- Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide.Antimicrobial agents and chemotherapy · 2012Article
- Modulation of substrate efflux in bacterial small multidrug resistance proteins by mutations at the dimer interface.Journal of bacteriology · 2011Article
- Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without detergents.Protein science : a publication of the Protein Society · 2011Article
- Expression of neurotransmitter transporters for structural and biochemical studies.Protein expression and purification · 2010Article
- Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes.PloS one · 2010Article
- Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters.The Journal of biological chemistry · 2010Article
- Efficacy of a potential trivalent vaccine based on Hc fragments of botulinum toxins A, B, and E produced in a cell-free expression system.Clinical and vaccine immunology : CVI · 2010Article
- An Escherichia coli-based cell-free system for large-scale production of functional mammalian membrane proteins suitable for X-ray crystallography.Journal of molecular microbiology and biotechnology · 2010Article
- Cell-free expression and stable isotope labelling strategies for membrane proteins.Journal of biomolecular NMR · 2010Article
- Production of functional bacteriorhodopsin by an Escherichia coli cell-free protein synthesis system supplemented with steroid detergent and lipid.Protein science : a publication of the Protein Society · 2009Article
- The assembly motif of a bacterial small multidrug resistance protein.The Journal of biological chemistry · 2009Article
- Parallel topology of genetically fused EmrE homodimers.The EMBO journal · 2008Article
- Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better.Biochimica et biophysica acta · 2007Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
EmrE is a small multidrug transporter from Escherichia coli that provides a unique model for the study of polytopic membrane proteins. Here, we show its synthesis in a cell-free system in a fully functional form. The detergent-solubilized protein binds substrates with high affinity and, when reconstituted into proteoliposomes, transports substrate in a Deltamicro(H)(+)-dependent fashion. Here, we used the cell-free system to study the oligomeric properties of EmrE. EmrE functions as an oligomer, but the size of the functional oligomer has not been established unequivocally. Coexpression of two plasmids in the cell-free system allowed demonstration of functional complementation and pull-down experiments confirmed that the basic functional unit is the dimer. An additional interaction between dimers has been detected by using crosslinking between unique Cys residues. This finding implies the existence of a dimer of dimers.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.