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Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants
Transport of most nuclear encoded mitochondrial proteins into mitochondria is mediated by heteropolymeric translocases in the membranes of the organelles. The t ranslocase of the o uter mitochondrial m embrane (TOM) was characterized in fungi, and it was shown that TOM from yeast comprises nine diff...
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Published in: | The Journal of biological chemistry 1998-07, Vol.273 (27), p.17251-17257 |
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container_end_page | 17257 |
container_issue | 27 |
container_start_page | 17251 |
container_title | The Journal of biological chemistry |
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creator | Jansch, L. (Universitat Hannover, Hannover, Germany.) Kruft, V Schmitz, U.K Braun, H.P |
description | Transport of most nuclear encoded mitochondrial proteins into mitochondria is mediated by heteropolymeric translocases in
the membranes of the organelles. The t ranslocase of the o uter mitochondrial m embrane (TOM) was characterized in fungi, and it was shown that TOM from yeast comprises nine different subunits. This publication
is the first report on the preparation of the TOM complex from plant mitochondria. The protein complex from potato was purified
by ( a ) blue native polyacrylamide gel electrophoresis and ( b ) by immunoaffinity chromatography. On blue native gels, the potato TOM complex runs close to cytochrome c oxidase at 230 kDa and hence only comprises about half of the size of fungal TOM complexes. Analysis of the TOM complex from
potato by SDS-polyacrylamide gel electrophoresis allows separation of seven different subunits of 70, 36, 23, 9, 8, 7, and
6 kDa. The 23-kDa protein is identical to the previously characterized potato TOM20 receptor, as shown by in vitro assembly of this protein into the 230-kDa complex, by immunoblotting and by direct protein sequencing. Partial amino acid
sequence data of the other subunits allowed us to identify sequence similarity between the 36-kDa protein and fungal TOM40.
Sequence analysis of cDNAs encoding the 7-kDa protein revealed significant sequence homology of this protein to TOM7 from
yeast. However, potato TOM7 has a N-terminal extension, which is very rich in basic amino acids. Counterparts to the TOM22
and TOM37 proteins from yeast seem to be absent in the potato TOM complex, whereas an additional low molecular mass subunit
occurs. Functional implications of these findings are discussed. |
doi_str_mv | 10.1074/jbc.273.27.17251 |
format | article |
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the membranes of the organelles. The t ranslocase of the o uter mitochondrial m embrane (TOM) was characterized in fungi, and it was shown that TOM from yeast comprises nine different subunits. This publication
is the first report on the preparation of the TOM complex from plant mitochondria. The protein complex from potato was purified
by ( a ) blue native polyacrylamide gel electrophoresis and ( b ) by immunoaffinity chromatography. On blue native gels, the potato TOM complex runs close to cytochrome c oxidase at 230 kDa and hence only comprises about half of the size of fungal TOM complexes. Analysis of the TOM complex from
potato by SDS-polyacrylamide gel electrophoresis allows separation of seven different subunits of 70, 36, 23, 9, 8, 7, and
6 kDa. The 23-kDa protein is identical to the previously characterized potato TOM20 receptor, as shown by in vitro assembly of this protein into the 230-kDa complex, by immunoblotting and by direct protein sequencing. Partial amino acid
sequence data of the other subunits allowed us to identify sequence similarity between the 36-kDa protein and fungal TOM40.
Sequence analysis of cDNAs encoding the 7-kDa protein revealed significant sequence homology of this protein to TOM7 from
yeast. However, potato TOM7 has a N-terminal extension, which is very rich in basic amino acids. Counterparts to the TOM22
and TOM37 proteins from yeast seem to be absent in the potato TOM complex, whereas an additional low molecular mass subunit
occurs. Functional implications of these findings are discussed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.27.17251</identifier><identifier>PMID: 9642296</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - isolation & purification ; Adenosine Triphosphatases - metabolism ; ADN ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Base Sequence ; BINDING PROTEINS ; CELL MEMBRANES ; CHEMICAL COMPOSITION ; Chromatography, Affinity - methods ; Cloning, Molecular ; COMPLEMENTARY DNA ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DNA ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli Proteins ; GENBANK/Y16228 ; Intracellular Membranes - enzymology ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; Membrane Transport Proteins ; MITOCHONDRIA ; Mitochondria - enzymology ; MITOCHONDRIE ; MITOCONDRIA ; MOLECULAR SEQUENCE DATA ; MOLECULAR WEIGHT ; NUCLEOTIDE SEQUENCE ; PESO MOLECULAR ; POIDS MOLECULAIRE ; PROTEINAS ; PROTEINAS AGLUTINANTES ; PROTEINE ; PROTEINE DE LIAISON ; PROTEINS ; PURIFICACION ; PURIFICATION ; SEC Translocation Channels ; SecA Proteins ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; SOLANUM TUBEROSUM ; Solanum tuberosum - enzymology ; SUBUNIT COMPOSITION</subject><ispartof>The Journal of biological chemistry, 1998-07, Vol.273 (27), p.17251-17257</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-409ddc78223a454a2bb4d1d582038fd776ad235ee63a2ae944dcc6f35baa90d53</citedby><cites>FETCH-LOGICAL-c418t-409ddc78223a454a2bb4d1d582038fd776ad235ee63a2ae944dcc6f35baa90d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9642296$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jansch, L. (Universitat Hannover, Hannover, Germany.)</creatorcontrib><creatorcontrib>Kruft, V</creatorcontrib><creatorcontrib>Schmitz, U.K</creatorcontrib><creatorcontrib>Braun, H.P</creatorcontrib><title>Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Transport of most nuclear encoded mitochondrial proteins into mitochondria is mediated by heteropolymeric translocases in
the membranes of the organelles. The t ranslocase of the o uter mitochondrial m embrane (TOM) was characterized in fungi, and it was shown that TOM from yeast comprises nine different subunits. This publication
is the first report on the preparation of the TOM complex from plant mitochondria. The protein complex from potato was purified
by ( a ) blue native polyacrylamide gel electrophoresis and ( b ) by immunoaffinity chromatography. On blue native gels, the potato TOM complex runs close to cytochrome c oxidase at 230 kDa and hence only comprises about half of the size of fungal TOM complexes. Analysis of the TOM complex from
potato by SDS-polyacrylamide gel electrophoresis allows separation of seven different subunits of 70, 36, 23, 9, 8, 7, and
6 kDa. The 23-kDa protein is identical to the previously characterized potato TOM20 receptor, as shown by in vitro assembly of this protein into the 230-kDa complex, by immunoblotting and by direct protein sequencing. Partial amino acid
sequence data of the other subunits allowed us to identify sequence similarity between the 36-kDa protein and fungal TOM40.
Sequence analysis of cDNAs encoding the 7-kDa protein revealed significant sequence homology of this protein to TOM7 from
yeast. However, potato TOM7 has a N-terminal extension, which is very rich in basic amino acids. Counterparts to the TOM22
and TOM37 proteins from yeast seem to be absent in the potato TOM complex, whereas an additional low molecular mass subunit
occurs. Functional implications of these findings are discussed.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - isolation & purification</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>BINDING PROTEINS</subject><subject>CELL MEMBRANES</subject><subject>CHEMICAL COMPOSITION</subject><subject>Chromatography, Affinity - methods</subject><subject>Cloning, Molecular</subject><subject>COMPLEMENTARY DNA</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DNA</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli Proteins</subject><subject>GENBANK/Y16228</subject><subject>Intracellular Membranes - enzymology</subject><subject>MEMBRANAS CELULARES</subject><subject>MEMBRANE CELLULAIRE</subject><subject>Membrane Transport Proteins</subject><subject>MITOCHONDRIA</subject><subject>Mitochondria - enzymology</subject><subject>MITOCHONDRIE</subject><subject>MITOCONDRIA</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>MOLECULAR WEIGHT</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PESO MOLECULAR</subject><subject>POIDS MOLECULAIRE</subject><subject>PROTEINAS</subject><subject>PROTEINAS AGLUTINANTES</subject><subject>PROTEINE</subject><subject>PROTEINE DE LIAISON</subject><subject>PROTEINS</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>SEC Translocation Channels</subject><subject>SecA Proteins</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>SOLANUM TUBEROSUM</subject><subject>Solanum tuberosum - enzymology</subject><subject>SUBUNIT COMPOSITION</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkL1vFDEQxS0ECpeEngbJBaLbw19rr0sUBYIUiSKclM547dmco_V6sX1C_Pcx3EGHGGk0xXvzNPND6DUlW0qUeP84ui1TvPWWKtbTZ2hDycA73tP752hDCKOdZv3wEp2X8khaCU3P0JmWgjEtN-jbbgnfD4BdimsqoYa04DThuge8ZlhzqhAWXLNdypycLfBHTYcKGcdQk9unxedgZxwhjs0JeMop4nW2Sy2X6MVk5wKvTvMC7T5ef7266W6_fPp89eG2c4IOtRNEe-_UwBi3oheWjaPw1PcDI3yYvFLSesZ7AMkts6CF8M7JifejtZr4nl-gd8fcdnN7qFQTQ3EwtyMgHYpRWkslpfyvkUohBqF5M5Kj0eVUSobJrDlEm38aSswv-qbRN41-a_Obflt5c8o-jBH834UT7qa_Per78LD_ETKYMTR-EP8RM9lk7EMOxezuqNaKaK4l4U-UN5b0</recordid><startdate>19980703</startdate><enddate>19980703</enddate><creator>Jansch, L. (Universitat Hannover, Hannover, Germany.)</creator><creator>Kruft, V</creator><creator>Schmitz, U.K</creator><creator>Braun, H.P</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19980703</creationdate><title>Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants</title><author>Jansch, L. (Universitat Hannover, Hannover, Germany.) ; Kruft, V ; Schmitz, U.K ; Braun, H.P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-409ddc78223a454a2bb4d1d582038fd776ad235ee63a2ae944dcc6f35baa90d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - isolation & purification</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>BINDING PROTEINS</topic><topic>CELL MEMBRANES</topic><topic>CHEMICAL COMPOSITION</topic><topic>Chromatography, Affinity - methods</topic><topic>Cloning, Molecular</topic><topic>COMPLEMENTARY DNA</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DNA</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli Proteins</topic><topic>GENBANK/Y16228</topic><topic>Intracellular Membranes - enzymology</topic><topic>MEMBRANAS CELULARES</topic><topic>MEMBRANE CELLULAIRE</topic><topic>Membrane Transport Proteins</topic><topic>MITOCHONDRIA</topic><topic>Mitochondria - enzymology</topic><topic>MITOCHONDRIE</topic><topic>MITOCONDRIA</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>MOLECULAR WEIGHT</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PESO MOLECULAR</topic><topic>POIDS MOLECULAIRE</topic><topic>PROTEINAS</topic><topic>PROTEINAS AGLUTINANTES</topic><topic>PROTEINE</topic><topic>PROTEINE DE LIAISON</topic><topic>PROTEINS</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>SEC Translocation Channels</topic><topic>SecA Proteins</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><topic>SOLANUM TUBEROSUM</topic><topic>Solanum tuberosum - enzymology</topic><topic>SUBUNIT COMPOSITION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jansch, L. (Universitat Hannover, Hannover, Germany.)</creatorcontrib><creatorcontrib>Kruft, V</creatorcontrib><creatorcontrib>Schmitz, U.K</creatorcontrib><creatorcontrib>Braun, H.P</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jansch, L. (Universitat Hannover, Hannover, Germany.)</au><au>Kruft, V</au><au>Schmitz, U.K</au><au>Braun, H.P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-07-03</date><risdate>1998</risdate><volume>273</volume><issue>27</issue><spage>17251</spage><epage>17257</epage><pages>17251-17257</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Transport of most nuclear encoded mitochondrial proteins into mitochondria is mediated by heteropolymeric translocases in
the membranes of the organelles. The t ranslocase of the o uter mitochondrial m embrane (TOM) was characterized in fungi, and it was shown that TOM from yeast comprises nine different subunits. This publication
is the first report on the preparation of the TOM complex from plant mitochondria. The protein complex from potato was purified
by ( a ) blue native polyacrylamide gel electrophoresis and ( b ) by immunoaffinity chromatography. On blue native gels, the potato TOM complex runs close to cytochrome c oxidase at 230 kDa and hence only comprises about half of the size of fungal TOM complexes. Analysis of the TOM complex from
potato by SDS-polyacrylamide gel electrophoresis allows separation of seven different subunits of 70, 36, 23, 9, 8, 7, and
6 kDa. The 23-kDa protein is identical to the previously characterized potato TOM20 receptor, as shown by in vitro assembly of this protein into the 230-kDa complex, by immunoblotting and by direct protein sequencing. Partial amino acid
sequence data of the other subunits allowed us to identify sequence similarity between the 36-kDa protein and fungal TOM40.
Sequence analysis of cDNAs encoding the 7-kDa protein revealed significant sequence homology of this protein to TOM7 from
yeast. However, potato TOM7 has a N-terminal extension, which is very rich in basic amino acids. Counterparts to the TOM22
and TOM37 proteins from yeast seem to be absent in the potato TOM complex, whereas an additional low molecular mass subunit
occurs. Functional implications of these findings are discussed.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9642296</pmid><doi>10.1074/jbc.273.27.17251</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | Elsevier ScienceDirect Journals |
subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism ADN Amino Acid Sequence AMINO ACID SEQUENCES Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Base Sequence BINDING PROTEINS CELL MEMBRANES CHEMICAL COMPOSITION Chromatography, Affinity - methods Cloning, Molecular COMPLEMENTARY DNA COMPOSICION QUIMICA COMPOSITION CHIMIQUE DNA Electrophoresis, Polyacrylamide Gel Escherichia coli Proteins GENBANK/Y16228 Intracellular Membranes - enzymology MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Transport Proteins MITOCHONDRIA Mitochondria - enzymology MITOCHONDRIE MITOCONDRIA MOLECULAR SEQUENCE DATA MOLECULAR WEIGHT NUCLEOTIDE SEQUENCE PESO MOLECULAR POIDS MOLECULAIRE PROTEINAS PROTEINAS AGLUTINANTES PROTEINE PROTEINE DE LIAISON PROTEINS PURIFICACION PURIFICATION SEC Translocation Channels SecA Proteins SECUENCIA NUCLEOTIDICA Sequence Homology, Amino Acid SEQUENCE NUCLEOTIDIQUE SOLANUM TUBEROSUM Solanum tuberosum - enzymology SUBUNIT COMPOSITION |
title | Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants |
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