Tim50, a novel component of the TIM23 preprotein translocase of mitochondria
The preprotein translocase of the inner membrane of mitochondria (TIM23 complex) is the main entry gate for proteins of the matrix and the inner membrane. We isolated the TIM23 complex of Neurospora crassa . Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans t...
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| Veröffentlicht in: | The EMBO journal 2003-02, Vol.22 (4), p.816-825 |
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| creator | Mokranjac, Dejana Paschen, Stefan A. Kozany, Christian Prokisch, Holger Hoppins, Suzanne C. Nargang, Frank E. Neupert, Walter Hell, Kai |
| description | The preprotein translocase of the inner membrane of mitochondria (TIM23 complex) is the main entry gate for proteins of the matrix and the inner membrane. We isolated the TIM23 complex of
Neurospora crassa
. Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans the inner membrane with a single transmembrane segment and exposes a large hydrophilic domain in the intermembrane space. Tim50 is essential for viability of yeast. Mitochondria from cells depleted of Tim50 displayed strongly reduced import kinetics of preproteins using the TIM23 complex. Tim50 could be cross‐linked to preproteins that were halted at the level of the translocase of the outer membrane (TOM complex) or spanning both TOM and TIM23 complexes. We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space. |
| doi_str_mv | 10.1093/emboj/cdg090 |
| format | Article |
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Neurospora crassa
. Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans the inner membrane with a single transmembrane segment and exposes a large hydrophilic domain in the intermembrane space. Tim50 is essential for viability of yeast. Mitochondria from cells depleted of Tim50 displayed strongly reduced import kinetics of preproteins using the TIM23 complex. Tim50 could be cross‐linked to preproteins that were halted at the level of the translocase of the outer membrane (TOM complex) or spanning both TOM and TIM23 complexes. We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/cdg090</identifier><identifier>PMID: 12574118</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Carrier Proteins - metabolism ; Electron Transport Complex IV ; EMBO20 ; import ; Membrane Proteins - metabolism ; Membrane Transport Proteins - isolation & purification ; Membrane Transport Proteins - metabolism ; Membranes ; mitochondria ; Mitochondria - metabolism ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Molecular Sequence Data ; Neurospora - metabolism ; Neurospora crassa ; Nuclear Proteins - metabolism ; Protein Transport - physiology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - isolation & purification ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Alignment ; TIM23 complex ; Tim50 ; translocation ; Yeasts</subject><ispartof>The EMBO journal, 2003-02, Vol.22 (4), p.816-825</ispartof><rights>European Molecular Biology Organization 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Feb 17, 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6470-75f716e7bfb609221e64ddb03f8dab58e2db96e576f3085f183355cd3e71b0733</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC145450/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC145450/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12574118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mokranjac, Dejana</creatorcontrib><creatorcontrib>Paschen, Stefan A.</creatorcontrib><creatorcontrib>Kozany, Christian</creatorcontrib><creatorcontrib>Prokisch, Holger</creatorcontrib><creatorcontrib>Hoppins, Suzanne C.</creatorcontrib><creatorcontrib>Nargang, Frank E.</creatorcontrib><creatorcontrib>Neupert, Walter</creatorcontrib><creatorcontrib>Hell, Kai</creatorcontrib><title>Tim50, a novel component of the TIM23 preprotein translocase of mitochondria</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The preprotein translocase of the inner membrane of mitochondria (TIM23 complex) is the main entry gate for proteins of the matrix and the inner membrane. We isolated the TIM23 complex of
Neurospora crassa
. Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans the inner membrane with a single transmembrane segment and exposes a large hydrophilic domain in the intermembrane space. Tim50 is essential for viability of yeast. Mitochondria from cells depleted of Tim50 displayed strongly reduced import kinetics of preproteins using the TIM23 complex. Tim50 could be cross‐linked to preproteins that were halted at the level of the translocase of the outer membrane (TOM complex) or spanning both TOM and TIM23 complexes. We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space.</description><subject>Amino Acid Sequence</subject><subject>Carrier Proteins - metabolism</subject><subject>Electron Transport Complex IV</subject><subject>EMBO20</subject><subject>import</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - isolation & purification</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Membranes</subject><subject>mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Membrane Transport Proteins</subject><subject>Mitochondrial Proteins</subject><subject>Molecular Sequence Data</subject><subject>Neurospora - metabolism</subject><subject>Neurospora crassa</subject><subject>Nuclear Proteins - metabolism</subject><subject>Protein Transport - physiology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - isolation & purification</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>TIM23 complex</subject><subject>Tim50</subject><subject>translocation</subject><subject>Yeasts</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkr1z1DAQxT0MDLkEOloYDwVVTFaWJdlFCvJBCHOB4g4oNbK9vtNhS0ayA_nvUfDNET4GKhX7e7tv9ymKnhB4SaCgR9iVdnNU1Sso4F40IxmHJAXB7kczSDlJMpIXe9G-9xsAYLkgD6M9kjKREZLPovlSdwwOYxUbe41tXNmutwbNENsmHtYYLy-vUhr3DntnB9QmHpwyvrWV8njLdHqw1dqa2mn1KHrQqNbj4-17EH14fb48fZPM319cnr6aJxXPBCSCNYJwFGVTcijSlCDP6roE2uS1KlmOaV0WHJngDYWcNSSnlLGqpihICYLSg-h46tuPZYd1Few61cre6U65G2mVlr9WjF7Llb2WJGMZg6B_sdU7-2VEP8hO-wrbVhm0o5eCQpgL2X9BUggBrGABfP4buLGjM-EIgWEpKwQXATqcoMpZ7x02O8cE5G2W8keWcsoy4M_ubvkT3oYXADYBX3WLN_9sJs-vTt6K4DT8gaBLJp0PErNCd8fs3408nXijhtHhbtAf_bQf8NuurNxnGbYWTH56dyF5vlicpR8X8oR-B4mG1Ks</recordid><startdate>20030217</startdate><enddate>20030217</enddate><creator>Mokranjac, Dejana</creator><creator>Paschen, Stefan A.</creator><creator>Kozany, Christian</creator><creator>Prokisch, Holger</creator><creator>Hoppins, Suzanne C.</creator><creator>Nargang, Frank E.</creator><creator>Neupert, Walter</creator><creator>Hell, Kai</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20030217</creationdate><title>Tim50, a novel component of the TIM23 preprotein translocase of mitochondria</title><author>Mokranjac, Dejana ; Paschen, Stefan A. ; Kozany, Christian ; Prokisch, Holger ; Hoppins, Suzanne C. ; Nargang, Frank E. ; Neupert, Walter ; Hell, Kai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6470-75f716e7bfb609221e64ddb03f8dab58e2db96e576f3085f183355cd3e71b0733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Carrier Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mokranjac, Dejana</au><au>Paschen, Stefan A.</au><au>Kozany, Christian</au><au>Prokisch, Holger</au><au>Hoppins, Suzanne C.</au><au>Nargang, Frank E.</au><au>Neupert, Walter</au><au>Hell, Kai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tim50, a novel component of the TIM23 preprotein translocase of mitochondria</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2003-02-17</date><risdate>2003</risdate><volume>22</volume><issue>4</issue><spage>816</spage><epage>825</epage><pages>816-825</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The preprotein translocase of the inner membrane of mitochondria (TIM23 complex) is the main entry gate for proteins of the matrix and the inner membrane. We isolated the TIM23 complex of
Neurospora crassa
. Besides Tim23 and Tim17, it contained a novel component, referred to as Tim50. Tim50 spans the inner membrane with a single transmembrane segment and exposes a large hydrophilic domain in the intermembrane space. Tim50 is essential for viability of yeast. Mitochondria from cells depleted of Tim50 displayed strongly reduced import kinetics of preproteins using the TIM23 complex. Tim50 could be cross‐linked to preproteins that were halted at the level of the translocase of the outer membrane (TOM complex) or spanning both TOM and TIM23 complexes. We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12574118</pmid><doi>10.1093/emboj/cdg090</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Carrier Proteins - metabolism Electron Transport Complex IV EMBO20 import Membrane Proteins - metabolism Membrane Transport Proteins - isolation & purification Membrane Transport Proteins - metabolism Membranes mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins Mitochondrial Proteins Molecular Sequence Data Neurospora - metabolism Neurospora crassa Nuclear Proteins - metabolism Protein Transport - physiology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - isolation & purification Saccharomyces cerevisiae Proteins - metabolism Sequence Alignment TIM23 complex Tim50 translocation Yeasts |
| title | Tim50, a novel component of the TIM23 preprotein translocase of mitochondria |
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