Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-06702-3
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Funding
- Ingvar Carlsson Award from the Swedish Foundation for Strategic Research
- Karolinska Faculty
- Swedish Research Council
- Knut and Alice Wallenberg Foundation
- EMBO through the Young Investigator Program
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Membrane bilayers are made up of a myriad of different lipids that regulate the functional activity, stability, and oligomerization of many membrane proteins. Despite their importance, screening the structural and functional impact of lipid-protein interactions to identify specific lipid requirements remains a major challenge. Here, we use the FSEC-TS assay to show cardiolipin-dependent stabilization of the dimeric sodium/proton antiporter NhaA, demonstrating its ability to detect specific protein-lipid interactions. Based on the principle of FSECTS, we then engineer a simple thermal-shift assay (GFP-TS), which facilitates the highthroughput screening of lipid-and ligand-interactions with membrane proteins. By comparing the thermostability of medically relevant eukaryotic membrane proteins and a selection of bacterial counterparts, we reveal that eukaryotic proteins appear to have evolved to be more dependent to the presence of specific lipids.
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