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Dimerisation of the Yeast K+ Translocation Protein Trk1 Depends on the K+ Concentration
Authors:Natalia Kulik  Deepika Kale  Karin Spurna  Katsiaryna Shamayeva  Fabian Hauser  Sandra Milic  Hannah Janout  Vasilina Zayats  Jaroslaw Jacak  Jost Ludwig
Affiliation:1.Institute of Microbiology of the Czech Academy of Sciences, Zamek 136, 3733 Nove Hrady, Czech Republic;2.School of Medical Engineering and Applied Social Sciences, University of Applied Sciences Upper Austria, Garnisonstr, 21, 4020 Linz, Austria;3.Bioinformatics, University of Applied Sciences Upper Austria, 4232 Hagenberg, Austria;4.Institute of Symbolic AI, Johannes Kepler University, 4040 Linz, Austria
Abstract:In baker’s yeast (Saccharomyces cerevisiae), Trk1, a member of the superfamily of K-transporters (SKT), is the main K+ uptake system under conditions when its concentration in the environment is low. Structurally, Trk1 is made up of four domains, each similar and homologous to a K-channel α subunit. Because most K-channels are proteins containing four channel-building α subunits, Trk1 could be functional as a monomer. However, related SKT proteins TrkH and KtrB were crystallised as dimers, and for Trk1, a tetrameric arrangement has been proposed based on molecular modelling. Here, based on Bimolecular Fluorescence Complementation experiments and single-molecule fluorescence microscopy combined with molecular modelling; we provide evidence that Trk1 can exist in the yeast plasma membrane as a monomer as well as a dimer. The association of monomers to dimers is regulated by the K+ concentration.
Keywords:K+ translocation   Saccharomyces cerevisiae   bimolecular fluorescence complementation   dimerisation   molecular modelling   MD simulation
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