ArticleScientific reports2017
Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Maltose and Maltotriose Transporters in Brewer'sInternational journal of molecular sciences · 2025Review
- Specialization Restricts the Evolutionary Paths Available to Yeast Sugar Transporters.Molecular biology and evolution · 2024Article
- Expression patterns ofApplied and environmental microbiology · 2024Article
- Specialization restricts the evolutionary paths available to yeast sugar transporters.bioRxiv : the preprint server for biology · 2024Article
- Review
- Evolution and functional diversification of yeast sugar transporters.Essays in biochemistry · 2023Article
- Activating alternative transport modes in a multidrug resistance efflux pump to confer chemical susceptibility.Nature communications · 2022Article
- Novel Evolutionary Engineering Approach to Alter Substrate Specificity of Disaccharide Transporter Mal11 inJournal of fungi (Basel, Switzerland) · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Weak Acid Permeation in Synthetic Lipid Vesicles and Across the Yeast Plasma Membrane.Biophysical journal · 2020Article
- EmrE reminds us to expect the unexpected in membrane transport.The Journal of general physiology · 2020Article
- Regulation and metabolic engineering strategies for permeases of Saccharomyces cerevisiae.World journal of microbiology & biotechnology · 2019Review
- Dissection of Protonation Sites for Antibacterial Recognition and Transport in QacA, a Multi-Drug Efflux Transporter.Journal of molecular biology · 2019Article
- In vivo recombination of Saccharomyces eubayanus maltose-transporter genes yields a chimeric transporter that enables maltotriose fermentation.PLoS genetics · 2019Article
- Article
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2 authors at 1 institution in 1 country.
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Abstract
Mal11 catalyzes proton-coupled maltose transport across the plasma membrane of Saccharomyces cerevisiae. We used structure-based design of mutants and a kinetic analysis of maltose transport to determine the energy coupling mechanism of transport. We find that wildtype Mal11 is extremely well coupled and allows yeast to rapidly accumulate maltose to dangerous levels, resulting under some conditions in self-lysis. Three protonatable residues lining the central membrane-embedded cavity of Mal11 were identified as having potential roles in proton translocation. We probed the mechanistic basis for proton coupling with uphill and downhill transport assays and found that single mutants can still accumulate maltose but with a lower coupling efficiency than the wildtype. Next, we combined the individual mutations and created double and triple mutants. We found some redundancy in the functions of the acidic residues in proton coupling and that no single residue is most critical for proton coupling to maltose uptake, unlike what is usually observed in related transporters. Importantly, the triple mutants were completely uncoupled but still fully active in downhill efflux and equilibrium exchange. Together, these results depict a concerted mechanism of proton transport in Mal11 involving multiple charged residues.
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