Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor
Protein import into yeast mitochondria is mediated by four integral outer membrane proteins which function as import receptors. These proteins (termed Mas20p, Mas22p, Mas37p and Mas70p) appear to exist as two subcomplexes: a Mas37p-Mas70p heterodimer and a less well characterized Mas20p-Mas22p compl...
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| Veröffentlicht in: | The EMBO journal 1996-03, Vol.15 (6), p.1231-1237 |
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| creator | Haucke, V Horst, M Schatz, G Lithgow, T |
| description | Protein import into yeast mitochondria is mediated by four integral outer membrane proteins which function as import receptors. These proteins (termed Mas20p, Mas22p, Mas37p and Mas70p) appear to exist as two subcomplexes: a Mas37p-Mas70p heterodimer and a less well characterized Mas20p-Mas22p complex. The subcomplexes interact functionally during protein import, but it has remained uncertain whether they are in direct contact with each other in vivo. Here we show that Mas20p and Mas70p can be cross-linked in intact mitochondria, or co-immunoprecipitated from digitonin-solubilized mitochondria. Furthermore, the cytosolic domains of these two proteins interact in the 'two-hybrid' system. Association of Mas20p and Mas70p is virtually abolished by a mutation in the single tetratricopeptide motif in Mas20p. This mutation specifically inhibits import of precursors that are first recognized by Mas37p-Mas70p and only then transferred to Mas20p-Mas22p. We conclude that the two receptor subcomplexes of the mitochondrial protein import receptor interact in vivo via their Mas20p and Mas70p subunits and that this interaction is functionally important. |
| doi_str_mv | 10.1002/j.1460-2075.1996.tb00464.x |
| format | Article |
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These proteins (termed Mas20p, Mas22p, Mas37p and Mas70p) appear to exist as two subcomplexes: a Mas37p-Mas70p heterodimer and a less well characterized Mas20p-Mas22p complex. The subcomplexes interact functionally during protein import, but it has remained uncertain whether they are in direct contact with each other in vivo. Here we show that Mas20p and Mas70p can be cross-linked in intact mitochondria, or co-immunoprecipitated from digitonin-solubilized mitochondria. Furthermore, the cytosolic domains of these two proteins interact in the 'two-hybrid' system. Association of Mas20p and Mas70p is virtually abolished by a mutation in the single tetratricopeptide motif in Mas20p. This mutation specifically inhibits import of precursors that are first recognized by Mas37p-Mas70p and only then transferred to Mas20p-Mas22p. We conclude that the two receptor subcomplexes of the mitochondrial protein import receptor interact in vivo via their Mas20p and Mas70p subunits and that this interaction is functionally important.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1996.tb00464.x</identifier><identifier>PMID: 8635455</identifier><language>eng</language><publisher>England</publisher><subject>amino acid sequences ; Base Sequence ; binding ; binding proteins ; binding sites ; Biological Transport ; cell membranes ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; interactions ; membrane proteins ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; mitochondria ; Mitochondria - chemistry ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial Membrane Transport Proteins ; mitochondrial outer membranes ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; protein transport ; receptors ; Receptors, Cytoplasmic and Nuclear ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins</subject><ispartof>The EMBO journal, 1996-03, Vol.15 (6), p.1231-1237</ispartof><rights>1996 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5024-fd93bb46c2924e232f2baf3b358f1e0dde0279acecd2c21a2ef5a1a2bd79fadf3</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/PMC450024/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC450024/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8635455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haucke, V</creatorcontrib><creatorcontrib>Horst, M</creatorcontrib><creatorcontrib>Schatz, G</creatorcontrib><creatorcontrib>Lithgow, T</creatorcontrib><title>Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Protein import into yeast mitochondria is mediated by four integral outer membrane proteins which function as import receptors. These proteins (termed Mas20p, Mas22p, Mas37p and Mas70p) appear to exist as two subcomplexes: a Mas37p-Mas70p heterodimer and a less well characterized Mas20p-Mas22p complex. The subcomplexes interact functionally during protein import, but it has remained uncertain whether they are in direct contact with each other in vivo. Here we show that Mas20p and Mas70p can be cross-linked in intact mitochondria, or co-immunoprecipitated from digitonin-solubilized mitochondria. Furthermore, the cytosolic domains of these two proteins interact in the 'two-hybrid' system. Association of Mas20p and Mas70p is virtually abolished by a mutation in the single tetratricopeptide motif in Mas20p. This mutation specifically inhibits import of precursors that are first recognized by Mas37p-Mas70p and only then transferred to Mas20p-Mas22p. We conclude that the two receptor subcomplexes of the mitochondrial protein import receptor interact in vivo via their Mas20p and Mas70p subunits and that this interaction is functionally important.</description><subject>amino acid sequences</subject><subject>Base Sequence</subject><subject>binding</subject><subject>binding proteins</subject><subject>binding sites</subject><subject>Biological Transport</subject><subject>cell membranes</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>interactions</subject><subject>membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>mitochondria</subject><subject>Mitochondria - chemistry</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Membrane Transport Proteins</subject><subject>mitochondrial outer membranes</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>protein transport</subject><subject>receptors</subject><subject>Receptors, Cytoplasmic and Nuclear</subject><subject>Repetitive Sequences, Nucleic Acid</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc9u1DAQxiMEKkvhERAWB24JtuMkm0ocStXyR604QM-WY493vUrsYDtL99n6cjhktYIjpxnrm-83Y31Z9pbggmBM3-8KwmqcU9xUBWnbuogdxqxmxcOTbHWSnmYrTGuSM7Jun2cvQthhjKt1Q86ys3VdVqyqVtnjnQgUj0hYhVLbpDZM3WRNDMhpFLeARu8iGIvMMDofkQcJY3R-lg8gQkSDiU5unVXeCGRsBC9kRPv0mO0RohfRG-nG5DMKEmEEkWwuGp3m0XLCBYJ9Uq0EpBNdoGDspge0hQR0uevNxg2QOKcLXmbPtOgDvDrW8-z-5vrH1ef89tunL1eXt7msMGW5Vm3ZdayWtKUMaEk17YQuu7JaawJYKcC0aYUEqaikRFDQlUilU02rhdLlefZh4Y5TN4CSYNOPej56Mwh_4E4Y_q9izZZv3J6zKqXFkv_d0e_dzwlC5IMJEvpeWHBT4M0aE1bW8-DFMii9C8GDPu0gmM_J8x2f4-VzvHxOnh-T5w_J_PrvK0_WY9RJv1z0X6aHw3-Q-fXdx69_-sR4szC0cFxsvAn8_jvFpMSkSoW25W8Z2c8V</recordid><startdate>19960315</startdate><enddate>19960315</enddate><creator>Haucke, V</creator><creator>Horst, M</creator><creator>Schatz, G</creator><creator>Lithgow, T</creator><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19960315</creationdate><title>Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor</title><author>Haucke, V ; Horst, M ; Schatz, G ; Lithgow, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5024-fd93bb46c2924e232f2baf3b358f1e0dde0279acecd2c21a2ef5a1a2bd79fadf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>amino acid sequences</topic><topic>Base Sequence</topic><topic>binding</topic><topic>binding proteins</topic><topic>binding sites</topic><topic>Biological Transport</topic><topic>cell membranes</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>interactions</topic><topic>membrane proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>mitochondria</topic><topic>Mitochondria - chemistry</topic><topic>Mitochondria - genetics</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial Membrane Transport Proteins</topic><topic>mitochondrial outer membranes</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>protein transport</topic><topic>receptors</topic><topic>Receptors, Cytoplasmic and Nuclear</topic><topic>Repetitive Sequences, Nucleic Acid</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - chemistry</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haucke, V</creatorcontrib><creatorcontrib>Horst, M</creatorcontrib><creatorcontrib>Schatz, G</creatorcontrib><creatorcontrib>Lithgow, T</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>MEDLINE - 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>Haucke, V</au><au>Horst, M</au><au>Schatz, G</au><au>Lithgow, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1996-03-15</date><risdate>1996</risdate><volume>15</volume><issue>6</issue><spage>1231</spage><epage>1237</epage><pages>1231-1237</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Protein import into yeast mitochondria is mediated by four integral outer membrane proteins which function as import receptors. These proteins (termed Mas20p, Mas22p, Mas37p and Mas70p) appear to exist as two subcomplexes: a Mas37p-Mas70p heterodimer and a less well characterized Mas20p-Mas22p complex. The subcomplexes interact functionally during protein import, but it has remained uncertain whether they are in direct contact with each other in vivo. Here we show that Mas20p and Mas70p can be cross-linked in intact mitochondria, or co-immunoprecipitated from digitonin-solubilized mitochondria. Furthermore, the cytosolic domains of these two proteins interact in the 'two-hybrid' system. Association of Mas20p and Mas70p is virtually abolished by a mutation in the single tetratricopeptide motif in Mas20p. This mutation specifically inhibits import of precursors that are first recognized by Mas37p-Mas70p and only then transferred to Mas20p-Mas22p. We conclude that the two receptor subcomplexes of the mitochondrial protein import receptor interact in vivo via their Mas20p and Mas70p subunits and that this interaction is functionally important.</abstract><cop>England</cop><pmid>8635455</pmid><doi>10.1002/j.1460-2075.1996.tb00464.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | amino acid sequences Base Sequence binding binding proteins binding sites Biological Transport cell membranes Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism interactions membrane proteins Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism mitochondria Mitochondria - chemistry Mitochondria - genetics Mitochondria - metabolism Mitochondrial Membrane Transport Proteins mitochondrial outer membranes Models, Molecular Molecular Sequence Data Mutation Protein Binding Protein Conformation protein transport receptors Receptors, Cytoplasmic and Nuclear Repetitive Sequences, Nucleic Acid Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins |
| title | Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: evidence for a single hetero-oligomeric receptor |
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