Complexome Profiling Identifies TMEM126B as a Component of the Mitochondrial Complex I Assembly Complex
Macromolecular complexes are essential players in numerous biological processes. They are often large, dynamic, and rather labile; approaches to study them are scarce. Covering masses up to ∼30 MDa, we separated the native complexome of rat heart mitochondria by blue-native and large-pore blue-nativ...
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| Veröffentlicht in: | Cell metabolism 2012-10, Vol.16 (4), p.538-549 |
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| creator | Heide, Heinrich Bleier, Lea Steger, Mirco Ackermann, Jörg Dröse, Stefan Schwamb, Bettina Zörnig, Martin Reichert, Andreas S. Koch, Ina Wittig, Ilka Brandt, Ulrich |
| description | Macromolecular complexes are essential players in numerous biological processes. They are often large, dynamic, and rather labile; approaches to study them are scarce. Covering masses up to ∼30 MDa, we separated the native complexome of rat heart mitochondria by blue-native and large-pore blue-native gel electrophoresis to analyze its constituents by mass spectrometry. Similarities in migration patterns allowed hierarchical clustering into interaction profiles representing a comprehensive analysis of soluble and membrane-bound complexes of an entire organelle. The power of this bottom-up approach was validated with well-characterized mitochondrial multiprotein complexes. TMEM126B was found to comigrate with known assembly factors of mitochondrial complex I, namely CIA30, Ecsit, and Acad9. We propose terming this complex mitochondrial complex I assembly (MCIA) complex. Furthermore, we demonstrate that TMEM126B is required for assembly of complex I. In summary, complexome profiling is a powerful and unbiased technique allowing the identification of previously overlooked components of large multiprotein complexes.
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► Multiprotein complexes up to a mass of 30 MDa are analyzed by proteomic profiling ► The power of complexome profiling is shown for mitochondrial multiprotein complexes ► TMEM126B is essential for the assembly of mitochondrial complex I ► TMEM126B is a subunit of the mitochondrial complex I assembly (MCIA) complex |
| doi_str_mv | 10.1016/j.cmet.2012.08.009 |
| format | Article |
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► Multiprotein complexes up to a mass of 30 MDa are analyzed by proteomic profiling ► The power of complexome profiling is shown for mitochondrial multiprotein complexes ► TMEM126B is essential for the assembly of mitochondrial complex I ► TMEM126B is a subunit of the mitochondrial complex I assembly (MCIA) complex</description><identifier>ISSN: 1550-4131</identifier><identifier>EISSN: 1932-7420</identifier><identifier>DOI: 10.1016/j.cmet.2012.08.009</identifier><identifier>PMID: 22982022</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Databases, Protein ; Electrophoresis, Gel, Two-Dimensional ; HEK293 Cells ; Humans ; Male ; Mass Spectrometry ; Membrane Proteins - antagonists & inhibitors ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mitochondria, Heart - metabolism ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - metabolism ; Proteomics ; Rats ; Rats, Wistar ; RNA Interference ; RNA, Small Interfering - metabolism</subject><ispartof>Cell metabolism, 2012-10, Vol.16 (4), p.538-549</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-fca65951a9d855b37958d4304b65ac28ec3b36fb19e5465445094d80505822f33</citedby><cites>FETCH-LOGICAL-c466t-fca65951a9d855b37958d4304b65ac28ec3b36fb19e5465445094d80505822f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1550413112003324$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22982022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Heide, Heinrich</creatorcontrib><creatorcontrib>Bleier, Lea</creatorcontrib><creatorcontrib>Steger, Mirco</creatorcontrib><creatorcontrib>Ackermann, Jörg</creatorcontrib><creatorcontrib>Dröse, Stefan</creatorcontrib><creatorcontrib>Schwamb, Bettina</creatorcontrib><creatorcontrib>Zörnig, Martin</creatorcontrib><creatorcontrib>Reichert, Andreas S.</creatorcontrib><creatorcontrib>Koch, Ina</creatorcontrib><creatorcontrib>Wittig, Ilka</creatorcontrib><creatorcontrib>Brandt, Ulrich</creatorcontrib><title>Complexome Profiling Identifies TMEM126B as a Component of the Mitochondrial Complex I Assembly Complex</title><title>Cell metabolism</title><addtitle>Cell Metab</addtitle><description>Macromolecular complexes are essential players in numerous biological processes. They are often large, dynamic, and rather labile; approaches to study them are scarce. Covering masses up to ∼30 MDa, we separated the native complexome of rat heart mitochondria by blue-native and large-pore blue-native gel electrophoresis to analyze its constituents by mass spectrometry. Similarities in migration patterns allowed hierarchical clustering into interaction profiles representing a comprehensive analysis of soluble and membrane-bound complexes of an entire organelle. The power of this bottom-up approach was validated with well-characterized mitochondrial multiprotein complexes. TMEM126B was found to comigrate with known assembly factors of mitochondrial complex I, namely CIA30, Ecsit, and Acad9. We propose terming this complex mitochondrial complex I assembly (MCIA) complex. Furthermore, we demonstrate that TMEM126B is required for assembly of complex I. In summary, complexome profiling is a powerful and unbiased technique allowing the identification of previously overlooked components of large multiprotein complexes.
[Display omitted]
► Multiprotein complexes up to a mass of 30 MDa are analyzed by proteomic profiling ► The power of complexome profiling is shown for mitochondrial multiprotein complexes ► TMEM126B is essential for the assembly of mitochondrial complex I ► TMEM126B is a subunit of the mitochondrial complex I assembly (MCIA) complex</description><subject>Animals</subject><subject>Databases, Protein</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Male</subject><subject>Mass Spectrometry</subject><subject>Membrane Proteins - antagonists & inhibitors</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mitochondria, Heart - metabolism</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Proteomics</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>RNA Interference</subject><subject>RNA, Small Interfering - metabolism</subject><issn>1550-4131</issn><issn>1932-7420</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1P3DAQhi1UBJTyBzhUPvaSdPxJLPVCV7SsxAoO9Gw5zgS8SuKtnUXl3-PVLhx7mtHMM680DyGXDGoGTH9f137EuebAeA1NDWCOyBkzgldXksOn0isFlWSCnZLPOa8BhBZGnJBTzk3DgfMz8rSI42bAf3FE-pBiH4YwPdFlh9Mc-oCZPq5uVozrn9Rl6uiOjlNZ0tjT-RnpKszRP8epS8EN9BBGl_Q6Zxzb4fV99IUc927IeHGo5-TPr5vHxW11d_97ubi-q7zUeq5677QyijnTNUq14sqoppMCZKuV87xBL1qh-5YZVFIrKRUY2TWgQDWc90Kck2_73E2Kf7eYZzuG7HEY3IRxmy0Do6TiRVBB-R71KeacsLebFEaXXgtkd4Lt2u4E251gC40tgsvR10P-th2x-zh5N1qAH3sAy5cvAZPNPuDksQsJ_Wy7GP6X_wbfBoqi</recordid><startdate>20121003</startdate><enddate>20121003</enddate><creator>Heide, Heinrich</creator><creator>Bleier, Lea</creator><creator>Steger, Mirco</creator><creator>Ackermann, Jörg</creator><creator>Dröse, Stefan</creator><creator>Schwamb, Bettina</creator><creator>Zörnig, Martin</creator><creator>Reichert, Andreas S.</creator><creator>Koch, Ina</creator><creator>Wittig, Ilka</creator><creator>Brandt, Ulrich</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>20121003</creationdate><title>Complexome Profiling Identifies TMEM126B as a Component of the Mitochondrial Complex I Assembly Complex</title><author>Heide, Heinrich ; Bleier, Lea ; Steger, Mirco ; Ackermann, Jörg ; Dröse, Stefan ; Schwamb, Bettina ; Zörnig, Martin ; Reichert, Andreas S. ; Koch, Ina ; Wittig, Ilka ; Brandt, Ulrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466t-fca65951a9d855b37958d4304b65ac28ec3b36fb19e5465445094d80505822f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Databases, Protein</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Male</topic><topic>Mass Spectrometry</topic><topic>Membrane Proteins - antagonists & inhibitors</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mitochondria, Heart - metabolism</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Proteomics</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>RNA Interference</topic><topic>RNA, Small Interfering - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heide, Heinrich</creatorcontrib><creatorcontrib>Bleier, Lea</creatorcontrib><creatorcontrib>Steger, Mirco</creatorcontrib><creatorcontrib>Ackermann, Jörg</creatorcontrib><creatorcontrib>Dröse, Stefan</creatorcontrib><creatorcontrib>Schwamb, Bettina</creatorcontrib><creatorcontrib>Zörnig, Martin</creatorcontrib><creatorcontrib>Reichert, Andreas S.</creatorcontrib><creatorcontrib>Koch, Ina</creatorcontrib><creatorcontrib>Wittig, Ilka</creatorcontrib><creatorcontrib>Brandt, Ulrich</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell metabolism</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heide, Heinrich</au><au>Bleier, Lea</au><au>Steger, Mirco</au><au>Ackermann, Jörg</au><au>Dröse, Stefan</au><au>Schwamb, Bettina</au><au>Zörnig, Martin</au><au>Reichert, Andreas S.</au><au>Koch, Ina</au><au>Wittig, Ilka</au><au>Brandt, Ulrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complexome Profiling Identifies TMEM126B as a Component of the Mitochondrial Complex I Assembly Complex</atitle><jtitle>Cell metabolism</jtitle><addtitle>Cell Metab</addtitle><date>2012-10-03</date><risdate>2012</risdate><volume>16</volume><issue>4</issue><spage>538</spage><epage>549</epage><pages>538-549</pages><issn>1550-4131</issn><eissn>1932-7420</eissn><abstract>Macromolecular complexes are essential players in numerous biological processes. They are often large, dynamic, and rather labile; approaches to study them are scarce. Covering masses up to ∼30 MDa, we separated the native complexome of rat heart mitochondria by blue-native and large-pore blue-native gel electrophoresis to analyze its constituents by mass spectrometry. Similarities in migration patterns allowed hierarchical clustering into interaction profiles representing a comprehensive analysis of soluble and membrane-bound complexes of an entire organelle. The power of this bottom-up approach was validated with well-characterized mitochondrial multiprotein complexes. TMEM126B was found to comigrate with known assembly factors of mitochondrial complex I, namely CIA30, Ecsit, and Acad9. We propose terming this complex mitochondrial complex I assembly (MCIA) complex. Furthermore, we demonstrate that TMEM126B is required for assembly of complex I. In summary, complexome profiling is a powerful and unbiased technique allowing the identification of previously overlooked components of large multiprotein complexes.
[Display omitted]
► Multiprotein complexes up to a mass of 30 MDa are analyzed by proteomic profiling ► The power of complexome profiling is shown for mitochondrial multiprotein complexes ► TMEM126B is essential for the assembly of mitochondrial complex I ► TMEM126B is a subunit of the mitochondrial complex I assembly (MCIA) complex</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22982022</pmid><doi>10.1016/j.cmet.2012.08.009</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Databases, Protein Electrophoresis, Gel, Two-Dimensional HEK293 Cells Humans Male Mass Spectrometry Membrane Proteins - antagonists & inhibitors Membrane Proteins - genetics Membrane Proteins - metabolism Mitochondria, Heart - metabolism Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Proteomics Rats Rats, Wistar RNA Interference RNA, Small Interfering - metabolism |
| title | Complexome Profiling Identifies TMEM126B as a Component of the Mitochondrial Complex I Assembly Complex |
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