Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins
Mitochondria consist of four compartments-outer membrane, intermembrane space, inner membrane, and matrix--with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We...
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| Veröffentlicht in: | Molecular biology of the cell 2006-03, Vol.17 (3), p.1436-1450 |
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| container_title | Molecular biology of the cell |
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| creator | Zahedi, Rene P Sickmann, Albert Boehm, Andreas M Winkler, Christiane Zufall, Nicole Schönfisch, Birgit Guiard, Bernard Pfanner, Nikolaus Meisinger, Chris |
| description | Mitochondria consist of four compartments-outer membrane, intermembrane space, inner membrane, and matrix--with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of approximately 85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjögren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments. |
| doi_str_mv | 10.1091/mbc.e05-08-0740 |
| format | Article |
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A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of approximately 85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjögren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>EISSN: 1059-1524</identifier><identifier>DOI: 10.1091/mbc.e05-08-0740</identifier><identifier>PMID: 16407407</identifier><language>eng</language><publisher>United States: American Society for Cell Biology</publisher><subject>Aldehyde Oxidoreductases ; Aldehyde Oxidoreductases - chemistry ; Amino Acid Sequence ; Biochemistry, Molecular Biology ; Electrophoresis, Gel, Two-Dimensional ; Genome, Fungal ; Genomics ; Humans ; Life Sciences ; Mitochondria ; Mitochondria - metabolism ; Mitochondrial Membranes ; Mitochondrial Membranes - metabolism ; Mitochondrial Proteins ; Mitochondrial Proteins - analysis ; Mitochondrial Proteins - chemistry ; Mitochondrial Proteins - metabolism ; Molecular Sequence Data ; Protein Precursors ; Protein Precursors - analysis ; Protein Precursors - chemistry ; Protein Precursors - classification ; Protein Precursors - metabolism ; Proteomics ; RNA, Messenger ; RNA, Messenger - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Saccharomyces cerevisiae Proteins - analysis ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Spectrometry, Mass, Electrospray Ionization ; Transport Vesicles ; Transport Vesicles - metabolism</subject><ispartof>Molecular biology of the cell, 2006-03, Vol.17 (3), p.1436-1450</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2006, The American Society for Cell Biology 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c568t-d66d9caffd65daba512db08fa81db6d92250746b0638be79c266aa49ffaa0bf73</citedby><cites>FETCH-LOGICAL-c568t-d66d9caffd65daba512db08fa81db6d92250746b0638be79c266aa49ffaa0bf73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1382330/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1382330/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16407407$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00168063$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Zahedi, Rene P</creatorcontrib><creatorcontrib>Sickmann, Albert</creatorcontrib><creatorcontrib>Boehm, Andreas M</creatorcontrib><creatorcontrib>Winkler, Christiane</creatorcontrib><creatorcontrib>Zufall, Nicole</creatorcontrib><creatorcontrib>Schönfisch, Birgit</creatorcontrib><creatorcontrib>Guiard, Bernard</creatorcontrib><creatorcontrib>Pfanner, Nikolaus</creatorcontrib><creatorcontrib>Meisinger, Chris</creatorcontrib><title>Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Mitochondria consist of four compartments-outer membrane, intermembrane space, inner membrane, and matrix--with crucial but distinct functions for numerous cellular processes. 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Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.</description><subject>Aldehyde Oxidoreductases</subject><subject>Aldehyde Oxidoreductases - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Biochemistry, Molecular Biology</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Genome, Fungal</subject><subject>Genomics</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Membranes</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>Mitochondrial Proteins</subject><subject>Mitochondrial Proteins - analysis</subject><subject>Mitochondrial Proteins - chemistry</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Protein Precursors</subject><subject>Protein Precursors - analysis</subject><subject>Protein Precursors - chemistry</subject><subject>Protein Precursors - classification</subject><subject>Protein Precursors - metabolism</subject><subject>Proteomics</subject><subject>RNA, Messenger</subject><subject>RNA, Messenger - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Saccharomyces cerevisiae Proteins - analysis</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Transport Vesicles</subject><subject>Transport Vesicles - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><issn>1059-1524</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUUuPFCEQJsaN-9CzN8PJxEPvQjfQ9MVks1HXZJL1oGdS0OBgmmYEepL590s7E1f3VKTqexT1IfSWkmtKBnoTtLm2hDdENqRn5AW6oEM3NIxL8bK-CR8aylt2ji5z_kUIZUz0r9A5FWyF9xdo_pZisTF4g2GG6ZB9xtHhsrX4YCEXHHyJZhvnMXmYcFyKTTjYoBPMFie7tzBlDMYsYZmg-DivdMB50WaC_Edsl-xudfFzfo3OXCXYN6d6hX58_vT97r7ZPHz5ene7aQwXsjSjEONgwLlR8BE0cNqOmkgHko66jtqW1_2FJqKT2vaDaYUAYINzAES7vrtCH4-6u0UHOxo7lwST2iUfIB1UBK_-n8x-q37GvaKdbLuOVIEPR4HtM9r97UatvXpMIav_nlbs-5NZir8Xm4sKPhs7TfVEccmKDpxxIVgF3hyBJsWck3V_lSlRa56q5qlqnopItQZUGe_-_ccT_hRg9wjAs6BI</recordid><startdate>20060301</startdate><enddate>20060301</enddate><creator>Zahedi, Rene P</creator><creator>Sickmann, Albert</creator><creator>Boehm, Andreas M</creator><creator>Winkler, Christiane</creator><creator>Zufall, Nicole</creator><creator>Schönfisch, Birgit</creator><creator>Guiard, Bernard</creator><creator>Pfanner, Nikolaus</creator><creator>Meisinger, Chris</creator><general>American Society for Cell Biology</general><general>The American Society for Cell Biology</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>M7N</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>20060301</creationdate><title>Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins</title><author>Zahedi, Rene P ; 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A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of approximately 85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjögren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. 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| subjects | Aldehyde Oxidoreductases Aldehyde Oxidoreductases - chemistry Amino Acid Sequence Biochemistry, Molecular Biology Electrophoresis, Gel, Two-Dimensional Genome, Fungal Genomics Humans Life Sciences Mitochondria Mitochondria - metabolism Mitochondrial Membranes Mitochondrial Membranes - metabolism Mitochondrial Proteins Mitochondrial Proteins - analysis Mitochondrial Proteins - chemistry Mitochondrial Proteins - metabolism Molecular Sequence Data Protein Precursors Protein Precursors - analysis Protein Precursors - chemistry Protein Precursors - classification Protein Precursors - metabolism Proteomics RNA, Messenger RNA, Messenger - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Proteins - analysis Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Spectrometry, Mass, Electrospray Ionization Transport Vesicles Transport Vesicles - metabolism |
| title | Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins |
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