ArticlePloS one2016
pH Regulation of Electrogenic Sugar/H+ Symport in MFS Sugar Permeases.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
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- Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chemiosmotic nutrient transport in synthetic cells powered by electrogenic antiport coupled to decarboxylation.Nature communications · 2024Article
- Study on the inhibitory activity and mechanism of Mentha haplocalyx essential oil nanoemulsion against Fusarium oxysporum growth.Scientific reports · 2024Article
- Functional Characterization of the Lysosomal Peptide/Histidine Transporter PHT1 (Biomolecules · 2024Article
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Functional promiscuity of small multidrug resistance transporters from Staphylococcus aureus, Pseudomonas aeruginosa, and Francisella tularensis.Molecular microbiology · 2024Article
- Deorphanizing solute carriers inFrontiers in microbiology · 2024Article
- A Comparative Study on the Lysosomal Cation Channel TMEM175 Using Automated Whole-Cell Patch-Clamp, Lysosomal Patch-Clamp, and Solid Supported Membrane-Based Electrophysiology: Functional Characterization and High-Throughput Screening Assay Development.International journal of molecular sciences · 2023Article
- Functional characterization of SGLT1 using SSM-based electrophysiology: Kinetics of sugar binding and translocation.Frontiers in physiology · 2023Article
- A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport.The Journal of biological chemistry · 2021Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Article
- Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter.Nature communications · 2020Article
- Transporter engineering in microbial cell factories: the ins, the outs, and the in-betweens.Current opinion in biotechnology · 2020Review
- AspThe Journal of biological chemistry · 2020Article
- Functional Characterization of SLC Transporters Using Solid Supported Membranes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- A channel profile report of the unusual KThe Journal of general physiology · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial sugar symporters in the Major Facilitator Superfamily (MFS) use the H+ (and in a few cases Na+) electrochemical gradients to achieve active transport of sugar into the cell. Because a number of structures of MFS sugar symporters have been solved recently, molecular insight into the transport mechanism is possible from detailed functional analysis. We present here a comparative electrophysiological study of the lactose permease (LacY), the fucose permease (FucP) and the xylose permease (XylE), which reveals common mechanistic principles and differences. In all three symporters energetically downhill electrogenic sugar/H+ symport is observed. Comparison of the pH dependence of symport at symmetrical pH exhibits broad bell-shaped pH profiles extending over 3 to 6 pH units and a decrease at extremely alkaline pH ≥ 9.4 and at acidic to neutral pH = 4.6-7.5. The pH dependence can be described by an acidic to neutral apparent pK (pKapp) and an alkaline pKapp. Experimental evidence suggests that the alkaline pKapp is due to H+ depletion at the protonation site, while the acidic pKapp is due to inhibition of deprotonation. Since previous studies suggest that a single carboxyl group in LacY (Glu325) may be the only side chain directly involved in H+ translocation and a carboxyl side chain with similar properties has been identified in FucP (Asp46) and XylE (Asp27), the present results imply that the pK of this residue is switched during H+/sugar symport in all three symporters.
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