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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| Published in: | Science (American Association for the Advancement of Science) Vol. 362; no. 6416; p. 829 |
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| Main Authors: | , , , , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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16.11.2018
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| ISSN: | 1095-9203, 1095-9203 |
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| 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
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. |
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| AbstractList | 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.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. 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. |
| Author | Khalid, Syma Samsudin, Firdaus Beilsten-Edmands, Victoria Matthews, Stephen J Wu, Di Gerle, Christoph Zeev-Ben-Mordehai, Tzviya Baker, Lindsay A Jiko, Chimari Robinson, Carol V Rouse, Sarah L Stewart, Alastair G Chorev, Dror S Grünewald, Kay |
| Author_xml | – sequence: 1 givenname: Dror S orcidid: 0000-0002-0751-0092 surname: Chorev fullname: Chorev, Dror S organization: Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK – sequence: 2 givenname: Lindsay A orcidid: 0000-0001-9578-4263 surname: Baker fullname: Baker, Lindsay A organization: Division of Structural Biology, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK – sequence: 3 givenname: Di surname: Wu fullname: Wu, Di organization: Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK – sequence: 4 givenname: Victoria surname: Beilsten-Edmands fullname: Beilsten-Edmands, Victoria organization: Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK – sequence: 5 givenname: Sarah L orcidid: 0000-0002-7115-1565 surname: Rouse fullname: Rouse, Sarah L organization: Department of Life Sciences, Imperial College, London, South Kensington Campus, London SW7 2AZ, UK – sequence: 6 givenname: Tzviya orcidid: 0000-0002-2571-550X surname: Zeev-Ben-Mordehai fullname: Zeev-Ben-Mordehai, Tzviya email: carol.robinson@chem.ox.ac.uk organization: Division of Structural Biology, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. carol.robinson@chem.ox.ac.uk – sequence: 7 givenname: Chimari surname: Jiko fullname: Jiko, Chimari organization: Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Japan – sequence: 8 givenname: Firdaus orcidid: 0000-0003-2766-4459 surname: Samsudin fullname: Samsudin, Firdaus organization: School of Chemistry, University of Southampton, University Road, Southampton SO17 1BJ, UK – sequence: 9 givenname: Christoph orcidid: 0000-0002-7265-2804 surname: Gerle fullname: Gerle, Christoph organization: Core Research for Evolutional Science and Technology, Japan and Science and Technology Agency, Kawaguchi, Japan – sequence: 10 givenname: Syma surname: Khalid fullname: Khalid, Syma organization: School of Chemistry, University of Southampton, University Road, Southampton SO17 1BJ, UK – sequence: 11 givenname: Alastair G orcidid: 0000-0002-2070-6030 surname: Stewart fullname: Stewart, Alastair G organization: Faculty of Medicine, The University of New South Wales, Sydney, NSW, Australia – sequence: 12 givenname: Stephen J orcidid: 0000-0003-0676-0927 surname: Matthews fullname: Matthews, Stephen J organization: Department of Life Sciences, Imperial College, London, South Kensington Campus, London SW7 2AZ, UK – sequence: 13 givenname: Kay orcidid: 0000-0002-4788-2691 surname: Grünewald fullname: Grünewald, Kay organization: Centre of Structural Systems Biology (CSSB), Notkestr. 85, D-22607, Heinrich-Pette Institute/University of Hamburg, Hamburg, Germany – sequence: 14 givenname: Carol V orcidid: 0000-0001-7829-5505 surname: Robinson fullname: Robinson, Carol V email: carol.robinson@chem.ox.ac.uk organization: Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK. carol.robinson@chem.ox.ac.uk |
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| ContentType | Journal Article |
| Copyright | Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. |
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| SubjectTerms | 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 |
| Title | Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry |
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