An engineered thermal-shift screen reveals specific lipid preferences of eukaryotic and prokaryotic membrane proteins.
Nat Commun
; 9(1): 4253, 2018 10 12.
Article
em En
| MEDLINE
| ID: mdl-30315156
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 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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Células Procarióticas
/
Células Eucarióticas
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article