Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions

We describe a general mass spectrometry approach to determine subunit stoichiometry and lipid binding in intact membrane protein complexes. By exploring conditions for preserving interactions during transmission into the gas phase and for optimally stripping away detergent, by subjecting the complex...

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Veröffentlicht in:Nature methods 2009-08, Vol.6 (8), p.585-587
Hauptverfasser: Bavro, Vassiliy N, Miguel, Ricardo Núñez, Schaedler, Theresia A, Robinson, Carol V, Zhou, Min, Barrera, Nelson P, van Veen, Hendrik W, Venter, Henrietta, Seeger, Markus A, Tate, Christopher G, Isaacson, Shoshanna C, Walmsley, Adrian R, Welch, Alex, Korkhov, Vladimir M
Format: Artikel
Sprache:eng
Schlagworte:
Biochemistry
Bioinformatics
Biological Microscopy
Biological Techniques
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
brief-communication
Cellular biology
Genetic aspects
Life Sciences
Lipids
Mass spectrometry
Membrane proteins
Membrane Transport Proteins - chemistry
Membranes
Multiprotein Complexes - chemistry
Physiological aspects
Protein Interaction Mapping
Protein Subunits - chemistry
Protein-protein interactions
Proteins
Proteomics
Proteomics - methods
Spectrometry, Mass, Electrospray Ionization - methods
Stoichiometry
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Beschreibung
Zusammenfassung:We describe a general mass spectrometry approach to determine subunit stoichiometry and lipid binding in intact membrane protein complexes. By exploring conditions for preserving interactions during transmission into the gas phase and for optimally stripping away detergent, by subjecting the complex to multiple collisions, we released the intact complex largely devoid of detergent. This enabled us to characterize both subunit stoichiometry and lipid binding in 4 membrane protein complexes.
ISSN:1548-7091
1548-7105
DOI:10.1038/nmeth.1347