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Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.

ABSTRACT: Membrane lipids act as solvents and functional cofactors for integral membrane proteins. The yeast plasma membrane is unusual in that it may have a high lipid order, which coincides with low passive permeability for small molecules and a slow lateral diffusion of proteins. Yet, membrane proteins whose functions require altered conformation must have flexibility within membranes. We have determined the molecular composition of yeast plasma membrane lipids located within a defined diameter of model proteins, including the APC-superfamily lysine transporter Lyp1. We now use the composition of lipids that naturally surround Lyp1 to guide testing of lipids that support the normal functioning of the transporter, when reconstituted in vesicles of defined lipid composition. We find that phosphatidylserine and ergosterol are essential for Lyp1 function, and the transport activity displays a sigmoidal relationship with the concentration of these lipids. Non-bilayer lipids stimulate transport activity, but different types are interchangeable. Remarkably, Lyp1 requires a relatively high fraction of lipids with one or more unsaturated acyl chains. The transport data and predictions of the periprotein lipidome of Lyp1 support a new model in which a narrow band of lipids immediately surrounding the transmembrane stalk of a model protein allows conformational changes in the protein.

SUBMITTER: van 't Klooster JS

PROVIDER: S-EPMC8005870 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:IntroductionProtein corona (PCN) adsorbed on the surface of nanoparticles has brought new research perspectives for the interaction between nanoparticles and microorganisms. In this study, the responses of saccharomyces cerevisiae' membrane lipid composition, the average length of the fatty acyl chains and the average number of unsaturation of fatty acids to ultrasound combined with nano-Fe3O4@PCN with time-limited proteolysis (nano-Fe3O4@TLP-PCN) was investigated.MethodsLipidomic data was obtained using Ultra-high performance liquid chromatography coupled with a Q-Exactive plus mass spectrometer. The membrane potential, proton motive force assay and the membrane lipid oxidation were measured using Di-BAC4(3), DISC3(5) and C11-BODIPY581/591 as the probes. Combined with the approach of feasible virtual samples generation, the back propagation artificial neural network (BP-ANN) model was adopted to establish the mapping relationship between lipids and membrane properties.ResultsThe time-limited proteolysis targeting wheat PCN-coated Fe3O4 nanoparticles resulted in regular changes of hydrodynamic diameters, ζ-potentials, and surface hydrophobicity. In addition, with the prolongation of PCN proteolysis time, disturbances of 3 S.cerevisiae membrane characteristics, and membrane lipidomic remodeling in response to ultrasound+ nano-Fe3O4@PCN were observed. The analysis of relative importance which followed revealed that ergosterol, phosphatidylserine, and phosphatidylinositol phosphate had the greatest influence on membrane potential. For membrane lipid oxidation, ceramide, phosphatidylethanolamine, and sitosterol ester contribute 16.2, 14.9, and 13.1%, respectively. The relative contributions of six lysolecithins to the dissipation of proton motive force remained limited.DiscussionAn adaptation mechanism of cell membrane to proteolyzed PCN, wherein lipidome remodeling could preserved functional membrane phenotypes was revealed. Furthermore, it is highlighted that the relative importances of SiE, Cer, PE and PIP in determining membrane potential, PMF dissipation and membrane lipid oxidation by establishing FVSG-BP-ANN model.

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Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.

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