Chorev, Dror S and Baker, Lindsay A and Wu, Di and Beilsten-Edmands, Victoria and Rouse, Sarah L and Zeev-Ben-Mordehai, Tzviya and Jiko, Chimari and Samsudin, Firdaus and Gerle, Christoph and Khalid, Syma and Stewart, Alastair G and Matthews, Stephen J and Grünewald, Kay and Robinson, Carol V (2018) Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry. Science, 362 (6416). pp.829-834. ISSN 0036-8075 (Not OA)
Full text not available from this repository.Abstract
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. In this work, we ejected intact assemblies from membranes, without chemical disruption, and used mass spectrometry to define their composition. From Escherichia coli outer membranes, we identified a chaperone-porin association and lipid interactions in the β-barrel assembly machinery. We observed efflux pumps bridging inner and outer membranes, and from inner membranes we identified a pentameric pore of TonB, as well as the protein-conducting channel SecYEG in association with F1FO adenosine triphosphate (ATP) synthase. Intact mitochondrial membranes from Bos taurus yielded respiratory complexes and fatty acid-bound dimers of the ADP (adenosine diphosphate)/ATP translocase (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.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 28 Nov 2018 05:57 |
| Last Modified: | 28 Nov 2018 05:57 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/774 |
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