Dimerisation of the Yeast K+Translocation Protein Trk1 Depends on the K+Concentration

0578992 - MBÚ 2024 RIV CH eng J - Journal Article
Kulik, Natalia - Kale, Deepika - Spurná, Karin - Shamayeva, Katsiaryna - Hauser, F. - Milic, S. - Janout, H. - Zayats, Vasilina - Jacak, J. - Ludwig, Jost
Dimerisation of the Yeast K+Translocation Protein Trk1 Depends on the K+Concentration.
International Journal of Molecular Sciences. Roč. 24, č. 1 (2023), č. článku 398. E-ISSN 1422-0067
R&D Projects: GA ČR(CZ) GA16-19221S; GA MŠMT(CZ) LM2015055; GA MŠMT(CZ) 8J22AT012
Institutional support: RVO:61388971
Keywords : affinity potassium-transport * saccharomyces-cerevisiae * crystal-structure * membrane-protein * gene disruption * channel * strains * network * encodes * systems * K+ translocation * Saccharomyces cerevisiae * bimolecular fluorescence complementation * dimerisation * molecular modelling * MD simulation
OECD category: Microbiology
Impact factor: 5.6, year: 2022
Method of publishing: Open access
https://www.mdpi.com/1422-0067/24/1/398

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 alpha subunit. Because most K-channels are proteins containing four channel-building alpha 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.
Permanent Link: https://hdl.handle.net/11104/0347893