ArticleThe Journal of biological chemistry2012
Antiparallel dimers of the small multidrug resistance protein EmrE are more stable than parallel dimers.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 51 citations in OpenAlex.
- Structure and inhibition mechanisms of Mycobacterium tuberculosis essential transporter efflux protein A.Nature communications · 2025Article
- Structural and biophysical analysis of aeLife · 2024Article
- Identification and expression of small multidrug resistance transporters in early-branching anaerobic fungi.Protein science : a publication of the Protein Society · 2023Article
- High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport.Nature communications · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Cooperativity and Steep Voltage Dependence in a Bacterial Channel.International journal of molecular sciences · 2019Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Influence of quaternary cation compound on the size of theBiochemistry and biophysics reports · 2018Article
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 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
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?Biochemistry · 2016Article
- Article
- Dual-topology insertion of a dual-topology membrane protein.Nature communications · 2015Article
- Blocking dynamics of the SMR transporter EmrE impairs efflux activity.Biophysical journal · 2014Article
- hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel transcription-dependent shuttling RNA-transporting complex.PloS one · 2014Article
- Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.Angewandte Chemie (International ed. in English) · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial multidrug transporter EmrE is a dual-topology membrane protein and as such is able to insert into the membrane in two opposite orientations. The functional form of EmrE is a homodimer; however, the relative orientation of the subunits in the dimer is under debate. Using EmrE variants with fixed, opposite orientations in the membrane, we now show that, although the proteins are able to form parallel dimers, an antiparallel organization of the subunits in the dimer is preferred. Blue-native PAGE analyses of intact oligomers and disulfide cross-linking demonstrate that in membranes, the proteins form parallel dimers only if no oppositely orientated partner is present. Co-expression of oppositely orientated proteins almost exclusively yields antiparallel dimers. Finally, parallel dimers can be disrupted and converted into antiparallel dimers by heating of detergent-solubilized protein. Importantly, in vivo function is correlated clearly to the presence of antiparallel dimers. Our results suggest that an antiparallel arrangement of the subunits in the dimer is more stable than a parallel organization and likely corresponds to the functional form of the protein.
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