An engineered thermal-shift screen reveals specific lipid preferences of eukaryotic and prokaryotic membrane proteins.

ABSTRACT: 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 FSEC-TS, we then engineer a simple thermal-shift assay (GFP-TS), which facilitates the high-throughput screening of lipid- and ligand- interactions with membrane proteins. By comparing the thermostability of medically relevant eukaryotic membrane prot

SUBMITTER: Nji E 

PROVIDER: S-EPMC6185904 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature