Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1
Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N-glycosylated protein anchored to the nuclear envelope-endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translo...
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| Veröffentlicht in: | FEMS yeast research 2010-09, Vol.10 (6), p.639-647 |
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| creator | Juanes, María Angeles Martínez-Garay, Carlos Andrés Igual, Juan Carlos Bañó, María Carmen |
| description | Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N-glycosylated protein anchored to the nuclear envelope-endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane domain were analyzed, suggesting the presence of an internal topogenic element that is capable of translocating Rot1 to the ER. To identify this sequence, we generated a combination of N- and C-terminal deletion mutants of Rot1 and we investigated their insertion into the membrane. The results show that two regions, amino acids 26-60 and 200-228, are involved in the post-translational translocation of Rot1 across the ER membrane. |
| doi_str_mv | 10.1111/j.1567-1364.2010.00653.x |
| format | Article |
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Rot1 is an N-glycosylated protein anchored to the nuclear envelope-endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane domain were analyzed, suggesting the presence of an internal topogenic element that is capable of translocating Rot1 to the ER. To identify this sequence, we generated a combination of N- and C-terminal deletion mutants of Rot1 and we investigated their insertion into the membrane. The results show that two regions, amino acids 26-60 and 200-228, are involved in the post-translational translocation of Rot1 across the ER membrane.</description><identifier>ISSN: 1567-1356</identifier><identifier>EISSN: 1567-1364</identifier><identifier>DOI: 10.1111/j.1567-1364.2010.00653.x</identifier><identifier>PMID: 20608986</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Actin ; Cell walls ; Clonal deletion ; Cytoskeleton ; Deletion mutant ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; Insertion ; Intracellular Membranes - metabolism ; membrane protein translocation ; Membrane Proteins - metabolism ; Molecular Chaperones - metabolism ; Post-translation ; Protein folding ; Protein Structure, Tertiary ; Protein Transport ; Proteins ; Recombination, Genetic ; Rot1 ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Deletion ; subcellular localization ; Translation</subject><ispartof>FEMS yeast research, 2010-09, Vol.10 (6), p.639-647</ispartof><rights>2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2010</rights><rights>2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4643-cab51afdd14957669ba1f513774f29cc2d4121746d5e86f5e323aa1d367dc72e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1567-1364.2010.00653.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1567-1364.2010.00653.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20608986$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Juanes, María Angeles</creatorcontrib><creatorcontrib>Martínez-Garay, Carlos Andrés</creatorcontrib><creatorcontrib>Igual, Juan Carlos</creatorcontrib><creatorcontrib>Bañó, María Carmen</creatorcontrib><title>Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1</title><title>FEMS yeast research</title><addtitle>FEMS Yeast Res</addtitle><description>Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N-glycosylated protein anchored to the nuclear envelope-endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane domain were analyzed, suggesting the presence of an internal topogenic element that is capable of translocating Rot1 to the ER. To identify this sequence, we generated a combination of N- and C-terminal deletion mutants of Rot1 and we investigated their insertion into the membrane. The results show that two regions, amino acids 26-60 and 200-228, are involved in the post-translational translocation of Rot1 across the ER membrane.</description><subject>Actin</subject><subject>Cell walls</subject><subject>Clonal deletion</subject><subject>Cytoskeleton</subject><subject>Deletion mutant</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Insertion</subject><subject>Intracellular Membranes - metabolism</subject><subject>membrane protein translocation</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Chaperones - metabolism</subject><subject>Post-translation</subject><subject>Protein folding</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Recombination, Genetic</subject><subject>Rot1</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sequence Deletion</subject><subject>subcellular localization</subject><subject>Translation</subject><issn>1567-1356</issn><issn>1567-1364</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kV1rHCEUhqW0NGnav5AIvcjVbHX8moHelJCkgUAhHxe9ElfPbFxmdKszSZb8-bjZdAst9caD53n04IsQpmRGy_qynFEhVUWZ5LOalFNCpGCzxzdof9d4u6uF3EMfcl4SQhUhzXu0VxNJmraR--jpxqQFjD4ssAkODzDMkwmAfciQRh9DqcaIxzvAEFxc9SYP3uJUFDv10_DHiB2-NtbemRSHtYWMLSS499mbouYMYfSmx6sUR_ABX8WRfkTvOtNn-PS6H6Dbs9Obk-_V5Y_zi5Nvl5XlkrPKmrmgpnOO8lYoKdu5oZ2gTCne1a21teO0popLJ6CRnQBWM2OoY1I5q2pgB-h4e295_NcEedSDzxb6vowdp6wVb1qmGJWF_PwXuYxTCmU4XTMmSCOl4oU6fKWm-QBOr5IfTFrr379agK9b4MH3sN71KdGb9PRSb4LRm5D0Jj39kp5-1Gc_r0pRdLbV47T6j1z9IxfraGt1JmqzSD7r2-tCMEKbhpBWsmc-w6bA</recordid><startdate>201009</startdate><enddate>201009</enddate><creator>Juanes, María Angeles</creator><creator>Martínez-Garay, Carlos Andrés</creator><creator>Igual, Juan Carlos</creator><creator>Bañó, María Carmen</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope></search><sort><creationdate>201009</creationdate><title>Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1</title><author>Juanes, María Angeles ; Martínez-Garay, Carlos Andrés ; Igual, Juan Carlos ; Bañó, María Carmen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4643-cab51afdd14957669ba1f513774f29cc2d4121746d5e86f5e323aa1d367dc72e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Actin</topic><topic>Cell walls</topic><topic>Clonal deletion</topic><topic>Cytoskeleton</topic><topic>Deletion mutant</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Insertion</topic><topic>Intracellular Membranes - metabolism</topic><topic>membrane protein translocation</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Chaperones - metabolism</topic><topic>Post-translation</topic><topic>Protein folding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Recombination, Genetic</topic><topic>Rot1</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Sequence Deletion</topic><topic>subcellular localization</topic><topic>Translation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Juanes, María Angeles</creatorcontrib><creatorcontrib>Martínez-Garay, Carlos Andrés</creatorcontrib><creatorcontrib>Igual, Juan Carlos</creatorcontrib><creatorcontrib>Bañó, María Carmen</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS yeast research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Juanes, María Angeles</au><au>Martínez-Garay, Carlos Andrés</au><au>Igual, Juan Carlos</au><au>Bañó, María Carmen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1</atitle><jtitle>FEMS yeast research</jtitle><addtitle>FEMS Yeast Res</addtitle><date>2010-09</date><risdate>2010</risdate><volume>10</volume><issue>6</issue><spage>639</spage><epage>647</epage><pages>639-647</pages><issn>1567-1356</issn><eissn>1567-1364</eissn><abstract>Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N-glycosylated protein anchored to the nuclear envelope-endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane domain were analyzed, suggesting the presence of an internal topogenic element that is capable of translocating Rot1 to the ER. To identify this sequence, we generated a combination of N- and C-terminal deletion mutants of Rot1 and we investigated their insertion into the membrane. The results show that two regions, amino acids 26-60 and 200-228, are involved in the post-translational translocation of Rot1 across the ER membrane.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>20608986</pmid><doi>10.1111/j.1567-1364.2010.00653.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEMS yeast research, 2010-09, Vol.10 (6), p.639-647 |
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| source | Wiley-Blackwell Journals; Oxford Journals Open Access Collection; MEDLINE; Alma/SFX Local Collection |
| subjects | Actin Cell walls Clonal deletion Cytoskeleton Deletion mutant Endoplasmic reticulum Endoplasmic Reticulum - metabolism Insertion Intracellular Membranes - metabolism membrane protein translocation Membrane Proteins - metabolism Molecular Chaperones - metabolism Post-translation Protein folding Protein Structure, Tertiary Protein Transport Proteins Recombination, Genetic Rot1 Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Sequence Deletion subcellular localization Translation |
| title | Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1 |
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