Chorev, Dror S., Baker, Lindsay A., Wu, Di, Beilsten-Edmands, Victoria, Rouse, Sarah L., Zeev-Ben-Mordehai, Tzviya, Jiko, Chimari, Samsudin, Firdaus, Gerle, Christoph, Khalid, Syma, Stewart, Alastair, Matthews, Stephen J., Grunewald, Kay and Robinson, Carol V. (2018) Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry. Science, 362 (6416), 829-834. (doi:10.1126/science.aau0976).
Abstract
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. Here we eject intact assemblies from membranes, without chemical disruption, and use mass spectrometry to define their composition. From E. coli outer membranes, we identify a chaperone-porin association and lipid interactions in the beta-barrel assembly machinery. Bridging inner and outer membranes we observe efflux pumps, and from inner membranes a pentameric pore of TonB, and the protein-conducting channel Sec YEG, in association with F1FO ATP-synthase. Intact mitochondrial membranes from Bos taurus yield respiratory complexes and fatty acid-bound dimers of the ADP/ATP transporter (ANT-1). These results highlight the importance of native membrane environments for retaining small-molecule binding, subunit interactions and associated chaperones of the membrane proteome.
More information
Identifiers
Catalogue record
Export record
Altmetrics
Contributors
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.