ArticleScientific reports2016
Asymmetry in inward- and outward-affinity constant of transport explain unidirectional lysine flux in Saccharomyces cerevisiae.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 221 citations in OpenAlex.
- Phenylalanine Versus Tyrosine (Pos. 367/332 in MCT1/MCT4) in the Substrate Binding Site Defines Affinity and Preferred Directionality of Human Monocarboxylate Transporters 1-4.Acta physiologica (Oxford, England) · 2026Article
- Intrinsic Asymmetry in Weak Acid Transmembrane Transporters.Biomolecules · 2026Review
- The Saccharomyces cerevisiae amino acid transporter Lyp1 has a broad substrate spectrum.FEBS letters · 2025Article
- The metabolic growth limitations of petite cells lacking the mitochondrial genome.Nature metabolism · 2021Article
- Growth Inhibition by Amino Acids inMicroorganisms · 2020Article
- Extracellular loops matter - subcellular location and function of the lysine transporter Lyp1 from Saccharomyces cerevisiae.The FEBS journal · 2020Article
- Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.Journal of molecular biology · 2020Article
- Periprotein lipidomes ofeLife · 2020Article
- Weak Acid Permeation in Synthetic Lipid Vesicles and Across the Yeast Plasma Membrane.Biophysical journal · 2020Article
- Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019Review
- Lysine harvesting is an antioxidant strategy and triggers underground polyamine metabolism.Nature · 2019Article
- Steric exclusion and protein conformation determine the localization of plasma membrane transporters.Nature communications · 2018Article
- New free-exchange model of EmrE transport.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae.Scientific reports · 2017Article
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7 authors at 2 institutions in 2 countries.
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Abstract
The import of basic amino acids in Saccharomyces cerevisiae has been reported to be unidirectional, which is not typical of how secondary transporters work. Since studies of energy coupling and transport kinetics are complicated in vivo, we purified the major lysine transporter (Lyp1) of yeast and reconstituted the protein into lipid vesicles. We show that the Michaelis constant (KM) of transport from out-to-in is well in the millimolar range and at least 3 to 4-orders of magnitude higher than that of transport in the opposite direction, disfavoring the efflux of solute via Lyp1. We also find that at low values of the proton motive force, the transport by Lyp1 is comparatively slow. We benchmarked the properties of eukaryotic Lyp1 to that of the prokaryotic homologue LysP and find that LysP has a similar KM for transport from in-to-out and out-to-in, consistent with rapid influx and efflux. We thus explain the previously described unidirectional nature of lysine transport in S. cerevisiae by the extraordinary kinetics of Lyp1 and provide a mechanism and rationale for previous observations. The high asymmetry in transport together with secondary storage in the vacuole allow the cell to accumulate basic amino acids to very high levels.
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