Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry

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 outer...

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Bibliographic Details
Published in:	Science (American Association for the Advancement of Science) Vol. 362; no. 6416; p. 829
Main Authors:	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 G, Matthews, Stephen J, Grünewald, Kay, Robinson, Carol V
Format:	Journal Article
Language:	English
Published:	United States 16.11.2018
Subjects:	Adenine Nucleotide Translocator 1 - chemistry Adenine Nucleotide Translocator 1 - metabolism Animals Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cattle Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Lipid Bilayers - chemistry Lipid Bilayers - metabolism Mass Spectrometry Membrane Proteins - chemistry Membrane Proteins - metabolism Mitochondrial Membranes - chemistry Mitochondrial Membranes - metabolism Mitochondrial Proton-Translocating ATPases - chemistry Mitochondrial Proton-Translocating ATPases - metabolism Molecular Chaperones - chemistry Molecular Chaperones - metabolism Porins - chemistry Porins - metabolism Protein Conformation, beta-Strand Proteome - chemistry Proteome - metabolism SEC Translocation Channels - chemistry SEC Translocation Channels - metabolism
ISSN:	1095-9203, 1095-9203
Online Access:	Get more information
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Summary:	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 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 F F adenosine triphosphate (ATP) synthase. Intact mitochondrial membranes from 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1095-9203 1095-9203
DOI:	10.1126/science.aau0976