TY - JOUR TI - Periprotein lipidomes of Saccharomyces cerevisiae provide a flexible environment for conformational changes of membrane proteins AU - van 't Klooster, Joury S AU - Cheng, Tan-Yun AU - Sikkema, Hendrik R AU - Jeucken, Aike AU - Moody, Branch AU - Poolman, Bert A2 - Dötsch, Volker A2 - Swartz, Kenton J VL - 9 PY - 2020 DA - 2020/04/17 SP - e57003 C1 - eLife 2020;9:e57003 DO - 10.7554/eLife.57003 UR - https://doi.org/10.7554/eLife.57003 AB - Yeast tolerates a low pH and high solvent concentrations. The permeability of the plasma membrane (PM) for small molecules is low and lateral diffusion of proteins is slow. These findings suggest a high degree of lipid order, which raises the question of how membrane proteins function in such an environment. The yeast PM is segregated into the Micro-Compartment-of-Can1 (MCC) and Pma1 (MCP), which have different lipid compositions. We extracted proteins from these microdomains via stoichiometric capture of lipids and proteins in styrene-maleic-acid-lipid-particles (SMALPs). We purified SMALP-lipid-protein complexes by chromatography and quantitatively analyzed periprotein lipids located within the diameter defined by one SMALP. Phospholipid and sterol concentrations are similar for MCC and MCP, but sphingolipids are enriched in MCP. Ergosterol is depleted from this periprotein lipidome, whereas phosphatidylserine is enriched relative to the bulk of the plasma membrane. Direct detection of PM lipids in the 'periprotein space' supports the conclusion that proteins function in the presence of a locally disordered lipid state. KW - lipidomics KW - plasma membrane KW - Saccharomyces cerevisiae KW - eisosome KW - membrane proteins KW - membrane domains JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -