Distinct Domains of Small Tims Involved in Subunit Interaction and Substrate Recognition
Tim9 and Tim10 belong to the small Tim family of mitochondrial ATP-independent chaperones. They are organised in a specific hetero-oligomeric complex (TIM10) that escorts polytopic proteins into the mitochondrial inner membrane. The contributions of the individual subunits to the assembly and functi...
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| Veröffentlicht in: | Journal of molecular biology 2005-08, Vol.351 (4), p.839-849 |
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| container_title | Journal of molecular biology |
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| creator | Vergnolle, Maïlys A.S. Baud, Catherine Golovanov, Alexander P. Alcock, Felicity Luciano, Pierre Lian, Lu-Yun Tokatlidis, Kostas |
| description | Tim9 and Tim10 belong to the small Tim family of mitochondrial ATP-independent chaperones. They are organised in a specific hetero-oligomeric complex (TIM10) that escorts polytopic proteins into the mitochondrial inner membrane. The contributions of the individual subunits to the assembly and function of the TIM10 complex remain poorly understood. Here, we show that substrate recognition and assembly of the complex are mediated by distinct domains of the subunits. These are unrelated to the characteristic “twin CX3C” motif that is present in all small Tims and ensures proper folding of the unassembled subunits. Specifically, we show that substrate recognition is achieved by the Tim10 subunit, whilst Tim9 serves a more structural role. The N-terminal domain of Tim10 is a substrate sensor whilst its C-terminal part is essential for complex formation. By contrast, both N and C-terminal domains of Tim9 are involved in the stability of the complex. |
| doi_str_mv | 10.1016/j.jmb.2005.06.010 |
| format | Article |
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They are organised in a specific hetero-oligomeric complex (TIM10) that escorts polytopic proteins into the mitochondrial inner membrane. The contributions of the individual subunits to the assembly and function of the TIM10 complex remain poorly understood. Here, we show that substrate recognition and assembly of the complex are mediated by distinct domains of the subunits. These are unrelated to the characteristic “twin CX3C” motif that is present in all small Tims and ensures proper folding of the unassembled subunits. Specifically, we show that substrate recognition is achieved by the Tim10 subunit, whilst Tim9 serves a more structural role. The N-terminal domain of Tim10 is a substrate sensor whilst its C-terminal part is essential for complex formation. 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They are organised in a specific hetero-oligomeric complex (TIM10) that escorts polytopic proteins into the mitochondrial inner membrane. The contributions of the individual subunits to the assembly and function of the TIM10 complex remain poorly understood. Here, we show that substrate recognition and assembly of the complex are mediated by distinct domains of the subunits. These are unrelated to the characteristic “twin CX3C” motif that is present in all small Tims and ensures proper folding of the unassembled subunits. Specifically, we show that substrate recognition is achieved by the Tim10 subunit, whilst Tim9 serves a more structural role. The N-terminal domain of Tim10 is a substrate sensor whilst its C-terminal part is essential for complex formation. By contrast, both N and C-terminal domains of Tim9 are involved in the stability of the complex.</description><subject>Base Sequence</subject><subject>chaperones</subject><subject>DNA, Fungal - genetics</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - genetics</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Membrane Transport Proteins</subject><subject>Mitochondrial Precursor Protein Import Complex Proteins</subject><subject>Mitochondrial Proteins - chemistry</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Multiprotein Complexes</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>protein assembly</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>small Tims</subject><subject>Surface Plasmon Resonance</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVJabZpf0AuRafc7IwkWyvRU8lHEwgUmhR6E7I8G7TYUirJC_330bILueU0MPO8L8xDyDmDlgGTl9t2Ow8tB-hbkC0w-EBWDJRulBTqhKwAOG-4EvKUfM55CxUUnfpETpkEoaXUK_L32ufigyv0Os7Wh0zjhj7Odprok58zvQ-7OO1wpD7Qx2VYgi91VzBZV3wM1IZxv88l2YL0N7r4XJF6-UI-buyU8etxnpE_tzdPV3fNw6-f91c_HhonelYauxmZFKDWVmsrpBKO93zNmV4PHMH2UotOY2e5ZuuuswL00HMYATtt0VktzsjFofclxX8L5mJmnx1Okw0Yl2yk6nqheF9BdgBdijkn3JiX5Geb_hsGZq_TbE3VafY6DUhTddbMt2P5Msw4viWO_irw_QBgfXHnMZnsPAaHo0_oihmjf6f-FYbthN8</recordid><startdate>20050826</startdate><enddate>20050826</enddate><creator>Vergnolle, Maïlys A.S.</creator><creator>Baud, Catherine</creator><creator>Golovanov, Alexander P.</creator><creator>Alcock, Felicity</creator><creator>Luciano, Pierre</creator><creator>Lian, Lu-Yun</creator><creator>Tokatlidis, Kostas</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>20050826</creationdate><title>Distinct Domains of Small Tims Involved in Subunit Interaction and Substrate Recognition</title><author>Vergnolle, Maïlys A.S. ; Baud, Catherine ; Golovanov, Alexander P. ; Alcock, Felicity ; Luciano, Pierre ; Lian, Lu-Yun ; Tokatlidis, Kostas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-afd163087a99a3683c25272197b2e0a569349e4a291744a309b520d0e49aeca93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Base Sequence</topic><topic>chaperones</topic><topic>DNA, Fungal - genetics</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Transport Proteins - chemistry</topic><topic>Membrane Transport Proteins - genetics</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial Membrane Transport Proteins</topic><topic>Mitochondrial Precursor Protein Import Complex Proteins</topic><topic>Mitochondrial Proteins - chemistry</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Multiprotein Complexes</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>protein assembly</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>small Tims</topic><topic>Surface Plasmon Resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vergnolle, Maïlys A.S.</creatorcontrib><creatorcontrib>Baud, Catherine</creatorcontrib><creatorcontrib>Golovanov, Alexander P.</creatorcontrib><creatorcontrib>Alcock, Felicity</creatorcontrib><creatorcontrib>Luciano, Pierre</creatorcontrib><creatorcontrib>Lian, Lu-Yun</creatorcontrib><creatorcontrib>Tokatlidis, Kostas</creatorcontrib><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>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vergnolle, Maïlys A.S.</au><au>Baud, Catherine</au><au>Golovanov, Alexander P.</au><au>Alcock, Felicity</au><au>Luciano, Pierre</au><au>Lian, Lu-Yun</au><au>Tokatlidis, Kostas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct Domains of Small Tims Involved in Subunit Interaction and Substrate Recognition</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2005-08-26</date><risdate>2005</risdate><volume>351</volume><issue>4</issue><spage>839</spage><epage>849</epage><pages>839-849</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Tim9 and Tim10 belong to the small Tim family of mitochondrial ATP-independent chaperones. They are organised in a specific hetero-oligomeric complex (TIM10) that escorts polytopic proteins into the mitochondrial inner membrane. The contributions of the individual subunits to the assembly and function of the TIM10 complex remain poorly understood. Here, we show that substrate recognition and assembly of the complex are mediated by distinct domains of the subunits. These are unrelated to the characteristic “twin CX3C” motif that is present in all small Tims and ensures proper folding of the unassembled subunits. Specifically, we show that substrate recognition is achieved by the Tim10 subunit, whilst Tim9 serves a more structural role. The N-terminal domain of Tim10 is a substrate sensor whilst its C-terminal part is essential for complex formation. By contrast, both N and C-terminal domains of Tim9 are involved in the stability of the complex.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>16039669</pmid><doi>10.1016/j.jmb.2005.06.010</doi><tpages>11</tpages></addata></record> |
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| subjects | Base Sequence chaperones DNA, Fungal - genetics Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins Mitochondrial Precursor Protein Import Complex Proteins Mitochondrial Proteins - chemistry Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Multiprotein Complexes Nuclear Magnetic Resonance, Biomolecular protein assembly Protein Structure, Tertiary Protein Subunits Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism small Tims Surface Plasmon Resonance |
| title | Distinct Domains of Small Tims Involved in Subunit Interaction and Substrate Recognition |
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