ArticleThe Journal of biological chemistry2010
Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Exploring Uniform, Dual, and Dynamic Topologies of Membrane Proteins by Substituted Cysteine Accessibility Method (SCAM™).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Transmembrane helices mediate the formation of a stable ternary complex of bCommunications biology · 2022Article
- An Interfacial Sodium Ion is an Essential Structural Feature of Fluc Family Fluoride Channels.Journal of molecular biology · 2020Article
- Dynamic membrane topology in an unassembled membrane protein.Nature chemical biology · 2019Article
- Protein Topology Prediction Algorithms Systematically Investigated in the Yeast Saccharomyces cerevisiae.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Comparison of the functional properties of trimeric and monomeric CaiT of Escherichia coli.Scientific reports · 2019Article
- Guanidinium export is the primal function of SMR family transporters.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Stable membrane orientations of small dual-topology membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Effects of mixed proximal and distal topogenic signals on the topological sensitivity of a membrane protein to the lipid environment.Biochimica et biophysica acta. Biomembranes · 2017Article
- Complete topology inversion can be part of normal membrane protein biogenesis.Protein science : a publication of the Protein Society · 2017Article
- Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?Biochemistry · 2016Article
- Dual-topology insertion of a dual-topology membrane protein.Nature communications · 2015Article
- Proof of dual-topology architecture of Fluc F- channels with monobody blockers.Nature communications · 2014Article
- Blocking dynamics of the SMR transporter EmrE impairs efflux activity.Biophysical journal · 2014Article
- Evolutionary mix-and-match with MFS transporters II.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Characterization and modeling of the oligomeric state and ligand binding behavior of purified translocator protein 18 kDa from Rhodobacter sphaeroides.Biochemistry · 2013Article
- New substrates on the block: clinically relevant resistances for EmrE and homologues.Journal of bacteriology · 2012Article
- Transforming a drug/H+ antiporter into a polyamine importer by a single mutation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Antiparallel dimers of the small multidrug resistance protein EmrE are more stable than parallel dimers.The Journal of biological chemistry · 2012Article
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4 authors.
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Abstract
Inverted repeats in ion-coupled transporters have evolved independently in many unrelated families. It has been suggested that this inverted symmetry is an essential element of the mechanism that allows for the conformational transitions in transporters. We show here that small multidrug transporters offer a model for the evolution of such repeats. This family includes both homodimers and closely related heterodimers. In the former, the topology determinants, evidently identical in each protomer, are weak, and we show that for EmrE, an homodimer from Escherichia coli, the insertion into the membrane is random, and dimers are functional whether they insert into the cytoplasmic membrane with the N- and C-terminal domains facing the inside or the outside of the cell. Also, mutants designed to insert with biased topology are functional regardless of the topology. In the case of EbrAB, a heterodimer homologue supposed to interact antiparallel, we show that one of the subunits, EbrB, can also function as a homodimer, most likely in a parallel mode. In addition, the EmrE homodimer can be forced to an antiparallel topology by fusion of an additional transmembrane segment. The simplicity of the mechanism of coupling ion and substrate transport and the few requirements for substrate recognition provide the robustness necessary to tolerate such a unique and unprecedented ambiguity in the interaction of the subunits and in the dimer topology relative to the membrane. The results suggest that the small multidrug transporters are at an evolutionary junction and provide a model for the evolution of structure of transport proteins.
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