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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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2018-11, Vol.362 (6416), p.829-834 |
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| creator | 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 |
| description | 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. |
| doi_str_mv | 10.1126/science.aau0976 |
| format | Article |
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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.</description><identifier>ISSN: 0036-8075</identifier><identifier>ISSN: 1095-9203</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aau0976</identifier><identifier>PMID: 30442809</identifier><language>eng</language><publisher>United States: The American Association for the Advancement of Science</publisher><subject>Adenine Nucleotide Translocator 1 - chemistry ; Adenine Nucleotide Translocator 1 - metabolism ; Adenosine ; Adenosine diphosphate ; Adenosine triphosphate ; Animals ; Assemblies ; ATP ; Bacteria ; Bacterial Outer Membrane Proteins - chemistry ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bos taurus ; Cattle ; Chaperones ; Dimers ; Disruption ; E coli ; Efflux ; Ejection ; Electron microscopy ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Inner membranes ; Lipid bilayers ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Lipids ; Mass Spectrometry ; Mass spectroscopy ; Membrane proteins ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membrane vesicles ; Membranes ; Mitochondria ; Mitochondrial Membranes - chemistry ; Mitochondrial Membranes - metabolism ; Mitochondrial Proton-Translocating ATPases - chemistry ; Mitochondrial Proton-Translocating ATPases - metabolism ; Molecular Chaperones - chemistry ; Molecular Chaperones - metabolism ; Organic chemistry ; Outer membranes ; Porins - chemistry ; Porins - metabolism ; Protein Conformation, beta-Strand ; Proteins ; Proteome - chemistry ; Proteome - metabolism ; Proteomes ; Scientific imaging ; SEC Translocation Channels - chemistry ; SEC Translocation Channels - metabolism ; Stoichiometry ; Translocase</subject><ispartof>Science (American Association for the Advancement of Science), 2018-11, Vol.362 (6416), p.829-834</ispartof><rights>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</rights><rights>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-b07d629fa26676cb98a884049c7ce831153ed6faef993e8733d2b6b7f3c52f1b3</citedby><cites>FETCH-LOGICAL-c524t-b07d629fa26676cb98a884049c7ce831153ed6faef993e8733d2b6b7f3c52f1b3</cites><orcidid>0000-0002-7115-1565 ; 0000-0002-2070-6030 ; 0000-0002-2571-550X ; 0000-0003-0676-0927 ; 0000-0003-2766-4459 ; 0000-0002-4788-2691 ; 0000-0001-9578-4263 ; 0000-0002-7265-2804 ; 0000-0001-7829-5505 ; 0000-0002-0751-0092</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,2871,2872,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30442809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chorev, Dror S</creatorcontrib><creatorcontrib>Baker, Lindsay A</creatorcontrib><creatorcontrib>Wu, Di</creatorcontrib><creatorcontrib>Beilsten-Edmands, Victoria</creatorcontrib><creatorcontrib>Rouse, Sarah L</creatorcontrib><creatorcontrib>Zeev-Ben-Mordehai, Tzviya</creatorcontrib><creatorcontrib>Jiko, Chimari</creatorcontrib><creatorcontrib>Samsudin, Firdaus</creatorcontrib><creatorcontrib>Gerle, Christoph</creatorcontrib><creatorcontrib>Khalid, Syma</creatorcontrib><creatorcontrib>Stewart, Alastair G</creatorcontrib><creatorcontrib>Matthews, Stephen J</creatorcontrib><creatorcontrib>Grünewald, Kay</creatorcontrib><creatorcontrib>Robinson, Carol V</creatorcontrib><title>Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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.</description><subject>Adenine Nucleotide Translocator 1 - chemistry</subject><subject>Adenine Nucleotide Translocator 1 - metabolism</subject><subject>Adenosine</subject><subject>Adenosine diphosphate</subject><subject>Adenosine triphosphate</subject><subject>Animals</subject><subject>Assemblies</subject><subject>ATP</subject><subject>Bacteria</subject><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bos taurus</subject><subject>Cattle</subject><subject>Chaperones</subject><subject>Dimers</subject><subject>Disruption</subject><subject>E coli</subject><subject>Efflux</subject><subject>Ejection</subject><subject>Electron microscopy</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Inner membranes</subject><subject>Lipid bilayers</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Lipids</subject><subject>Mass Spectrometry</subject><subject>Mass spectroscopy</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane vesicles</subject><subject>Membranes</subject><subject>Mitochondria</subject><subject>Mitochondrial Membranes - chemistry</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>Mitochondrial Proton-Translocating ATPases - chemistry</subject><subject>Mitochondrial Proton-Translocating ATPases - metabolism</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular Chaperones - metabolism</subject><subject>Organic chemistry</subject><subject>Outer membranes</subject><subject>Porins - chemistry</subject><subject>Porins - metabolism</subject><subject>Protein Conformation, beta-Strand</subject><subject>Proteins</subject><subject>Proteome - chemistry</subject><subject>Proteome - metabolism</subject><subject>Proteomes</subject><subject>Scientific imaging</subject><subject>SEC Translocation Channels - chemistry</subject><subject>SEC Translocation Channels - metabolism</subject><subject>Stoichiometry</subject><subject>Translocase</subject><issn>0036-8075</issn><issn>1095-9203</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtP3DAUhS1ExQyUNTtkiU03AT8SJ95UqkYFKo0EC7q2HOeaepTEUztBzL_vRTNFLRs_dL9z5ONDyAVn15wLdZNdgNHBtbUz07U6IkvOdFVoweQxWTImVdGwulqQ05w3jOFMyxOykKwsRcP0kpjHFCcII7U5w9D2ATKFDbgJOtqFhId-R32KAx3tFF6ADkglOyK2C9B31MVh28Mr3n1MdEAbmrcoQwlMafeZfPK2z3B-2M_Iz9vvT6v7Yv1w92P1bV24SpRT0bK6U0J7K5SqlWt1Y5umZKV2tYNGcl5J6JS34LWW0NRSdqJVbe0l6j1v5Rn5uvfdzu0AnYNxSrY32xQGm3Ym2mD-n4zhl3mOL0ZVQshSocGXg0GKv2fIkxlCdtD3mDXO2QguK45_LgWiVx_QTZzTiPHeKKlxYRqpmz3lUsw5gX9_DGfmrTxzKM8cykPF5b8Z3vm_bck_fsqaew</recordid><startdate>20181116</startdate><enddate>20181116</enddate><creator>Chorev, Dror S</creator><creator>Baker, Lindsay A</creator><creator>Wu, Di</creator><creator>Beilsten-Edmands, Victoria</creator><creator>Rouse, Sarah L</creator><creator>Zeev-Ben-Mordehai, Tzviya</creator><creator>Jiko, Chimari</creator><creator>Samsudin, Firdaus</creator><creator>Gerle, Christoph</creator><creator>Khalid, Syma</creator><creator>Stewart, Alastair G</creator><creator>Matthews, Stephen J</creator><creator>Grünewald, Kay</creator><creator>Robinson, Carol V</creator><general>The American Association for the Advancement of Science</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7115-1565</orcidid><orcidid>https://orcid.org/0000-0002-2070-6030</orcidid><orcidid>https://orcid.org/0000-0002-2571-550X</orcidid><orcidid>https://orcid.org/0000-0003-0676-0927</orcidid><orcidid>https://orcid.org/0000-0003-2766-4459</orcidid><orcidid>https://orcid.org/0000-0002-4788-2691</orcidid><orcidid>https://orcid.org/0000-0001-9578-4263</orcidid><orcidid>https://orcid.org/0000-0002-7265-2804</orcidid><orcidid>https://orcid.org/0000-0001-7829-5505</orcidid><orcidid>https://orcid.org/0000-0002-0751-0092</orcidid></search><sort><creationdate>20181116</creationdate><title>Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-b07d629fa26676cb98a884049c7ce831153ed6faef993e8733d2b6b7f3c52f1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adenine Nucleotide Translocator 1 - chemistry</topic><topic>Adenine Nucleotide Translocator 1 - metabolism</topic><topic>Adenosine</topic><topic>Adenosine diphosphate</topic><topic>Adenosine triphosphate</topic><topic>Animals</topic><topic>Assemblies</topic><topic>ATP</topic><topic>Bacteria</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bos taurus</topic><topic>Cattle</topic><topic>Chaperones</topic><topic>Dimers</topic><topic>Disruption</topic><topic>E coli</topic><topic>Efflux</topic><topic>Ejection</topic><topic>Electron microscopy</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Inner membranes</topic><topic>Lipid bilayers</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Lipids</topic><topic>Mass Spectrometry</topic><topic>Mass spectroscopy</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane vesicles</topic><topic>Membranes</topic><topic>Mitochondria</topic><topic>Mitochondrial Membranes - chemistry</topic><topic>Mitochondrial Membranes - metabolism</topic><topic>Mitochondrial Proton-Translocating ATPases - chemistry</topic><topic>Mitochondrial Proton-Translocating ATPases - metabolism</topic><topic>Molecular Chaperones - chemistry</topic><topic>Molecular Chaperones - metabolism</topic><topic>Organic chemistry</topic><topic>Outer membranes</topic><topic>Porins - chemistry</topic><topic>Porins - metabolism</topic><topic>Protein Conformation, beta-Strand</topic><topic>Proteins</topic><topic>Proteome - chemistry</topic><topic>Proteome - metabolism</topic><topic>Proteomes</topic><topic>Scientific imaging</topic><topic>SEC Translocation Channels - chemistry</topic><topic>SEC Translocation Channels - metabolism</topic><topic>Stoichiometry</topic><topic>Translocase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chorev, Dror S</creatorcontrib><creatorcontrib>Baker, Lindsay A</creatorcontrib><creatorcontrib>Wu, Di</creatorcontrib><creatorcontrib>Beilsten-Edmands, Victoria</creatorcontrib><creatorcontrib>Rouse, Sarah L</creatorcontrib><creatorcontrib>Zeev-Ben-Mordehai, Tzviya</creatorcontrib><creatorcontrib>Jiko, Chimari</creatorcontrib><creatorcontrib>Samsudin, Firdaus</creatorcontrib><creatorcontrib>Gerle, Christoph</creatorcontrib><creatorcontrib>Khalid, Syma</creatorcontrib><creatorcontrib>Stewart, Alastair G</creatorcontrib><creatorcontrib>Matthews, Stephen J</creatorcontrib><creatorcontrib>Grünewald, Kay</creatorcontrib><creatorcontrib>Robinson, Carol V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - 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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.</abstract><cop>United States</cop><pub>The American Association for the Advancement of Science</pub><pmid>30442809</pmid><doi>10.1126/science.aau0976</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-7115-1565</orcidid><orcidid>https://orcid.org/0000-0002-2070-6030</orcidid><orcidid>https://orcid.org/0000-0002-2571-550X</orcidid><orcidid>https://orcid.org/0000-0003-0676-0927</orcidid><orcidid>https://orcid.org/0000-0003-2766-4459</orcidid><orcidid>https://orcid.org/0000-0002-4788-2691</orcidid><orcidid>https://orcid.org/0000-0001-9578-4263</orcidid><orcidid>https://orcid.org/0000-0002-7265-2804</orcidid><orcidid>https://orcid.org/0000-0001-7829-5505</orcidid><orcidid>https://orcid.org/0000-0002-0751-0092</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2018-11, Vol.362 (6416), p.829-834 |
| issn | 0036-8075 1095-9203 1095-9203 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6522346 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Adenine Nucleotide Translocator 1 - chemistry Adenine Nucleotide Translocator 1 - metabolism Adenosine Adenosine diphosphate Adenosine triphosphate Animals Assemblies ATP Bacteria Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bos taurus Cattle Chaperones Dimers Disruption E coli Efflux Ejection Electron microscopy Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Inner membranes Lipid bilayers Lipid Bilayers - chemistry Lipid Bilayers - metabolism Lipids Mass Spectrometry Mass spectroscopy Membrane proteins Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane vesicles Membranes Mitochondria Mitochondrial Membranes - chemistry Mitochondrial Membranes - metabolism Mitochondrial Proton-Translocating ATPases - chemistry Mitochondrial Proton-Translocating ATPases - metabolism Molecular Chaperones - chemistry Molecular Chaperones - metabolism Organic chemistry Outer membranes Porins - chemistry Porins - metabolism Protein Conformation, beta-Strand Proteins Proteome - chemistry Proteome - metabolism Proteomes Scientific imaging SEC Translocation Channels - chemistry SEC Translocation Channels - metabolism Stoichiometry Translocase |
| title | Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T06%3A28%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20assemblies%20ejected%20directly%20from%20native%20membranes%20yield%20complexes%20for%20mass%20spectrometry&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Chorev,%20Dror%20S&rft.date=2018-11-16&rft.volume=362&rft.issue=6416&rft.spage=829&rft.epage=834&rft.pages=829-834&rft.issn=0036-8075&rft.eissn=1095-9203&rft_id=info:doi/10.1126/science.aau0976&rft_dat=%3Cproquest_pubme%3E2135111232%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2133921309&rft_id=info:pmid/30442809&rfr_iscdi=true |