Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids
Identifieur interne : 000D54 ( Istex/Corpus ); précédent : 000D53; suivant : 000D55Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids
Auteurs : Igor V. Kurochkin ; Yumi Mizuno ; Akihiko Konagaya ; Yoshiyuki Sakaki ; Christian Schönbach ; Yasushi OkazakiSource :
- The EMBO Journal [ 0261-4189 ] ; 2007-02-07.
Abstract
Peroxisomes play an important role in β‐oxidation of fatty acids. All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1‐mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of β‐oxidation.
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DOI: 10.1038/sj.emboj.7601525
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Kurochkin</name><affiliation><mods:affiliation>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</mods:affiliation></affiliation></author><author><name sortKey="Mizuno, Yumi" sort="Mizuno, Yumi" uniqKey="Mizuno Y" first="Yumi" last="Mizuno">Yumi Mizuno</name><affiliation><mods:affiliation>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</mods:affiliation></affiliation></author><author><name sortKey="Konagaya, Akihiko" sort="Konagaya, Akihiko" uniqKey="Konagaya A" first="Akihiko" last="Konagaya">Akihiko Konagaya</name><affiliation><mods:affiliation>RIKEN Genomic Sciences Center, Yokohama, Japan</mods:affiliation></affiliation></author><author><name sortKey="Sakaki, Yoshiyuki" sort="Sakaki, Yoshiyuki" uniqKey="Sakaki Y" first="Yoshiyuki" last="Sakaki">Yoshiyuki Sakaki</name><affiliation><mods:affiliation>Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, Yokohama, Japan</mods:affiliation></affiliation></author><author><name sortKey="Schonbach, Christian" sort="Schonbach, Christian" uniqKey="Schonbach C" first="Christian" last="Schönbach">Christian Schönbach</name><affiliation><mods:affiliation>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</mods:affiliation></affiliation></author><author><name sortKey="Okazaki, Yasushi" sort="Okazaki, Yasushi" uniqKey="Okazaki Y" first="Yasushi" last="Okazaki">Yasushi Okazaki</name><affiliation><mods:affiliation>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A4EF349C681091C1E3681A33814CFCCCDBA85C97</idno><date when="2007" year="2007">2007</date><idno type="doi">10.1038/sj.emboj.7601525</idno><idno type="url">https://api.istex.fr/document/A4EF349C681091C1E3681A33814CFCCCDBA85C97/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000D54</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids</title><author><name sortKey="Kurochkin, Igor V" sort="Kurochkin, Igor V" uniqKey="Kurochkin I" first="Igor V" last="Kurochkin">Igor V. 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All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1‐mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of β‐oxidation.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Igor V Kurochkin</name><affiliations><json:string>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</json:string></affiliations></json:item><json:item><name>Yumi Mizuno</name><affiliations><json:string>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</json:string></affiliations></json:item><json:item><name>Akihiko Konagaya</name><affiliations><json:string>RIKEN Genomic Sciences Center, Yokohama, Japan</json:string></affiliations></json:item><json:item><name>Yoshiyuki Sakaki</name><affiliations><json:string>Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, Yokohama, Japan</json:string></affiliations></json:item><json:item><name>Christian Schönbach</name><affiliations><json:string>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</json:string></affiliations></json:item><json:item><name>Yasushi Okazaki</name><affiliations><json:string>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>fatty acid oxidation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>peroxisomes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>protease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>protein processing</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Tysnd1</value></json:item></subject><articleId><json:string>EMBJ7601525</json:string></articleId><language><json:string>eng</json:string></language><abstract>Peroxisomes play an important role in β‐oxidation of fatty acids. All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. 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Japan</affiliation></author><author><persName><forename type="first">Akihiko</forename><surname>Konagaya</surname></persName><affiliation>RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation></author><author><persName><forename type="first">Yoshiyuki</forename><surname>Sakaki</surname></persName><affiliation>Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation></author><author><persName><forename type="first">Christian</forename><surname>Schönbach</surname></persName><note type="biography">Present address: Division of Genomics and Genetics, School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore</note><affiliation>Present address: Division of Genomics and Genetics, School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore</affiliation><affiliation>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation></author><author><persName><forename type="first">Yasushi</forename><surname>Okazaki</surname></persName><affiliation>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</affiliation></author></analytic><monogr><title level="j">The EMBO Journal</title><idno type="pISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><idno type="DOI">10.1002/(ISSN)1460-2075</idno><imprint><publisher>John Wiley & Sons, Ltd</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2007-02-07"></date><biblScope unit="volume">26</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="835">835</biblScope><biblScope unit="page" to="845">845</biblScope></imprint></monogr><idno type="istex">A4EF349C681091C1E3681A33814CFCCCDBA85C97</idno><idno type="DOI">10.1038/sj.emboj.7601525</idno><idno 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All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1‐mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of β‐oxidation.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>fatty acid oxidation</term></item><item><term>peroxisomes</term></item><item><term>protease</term></item><item><term>protein processing</term></item><item><term>Tysnd1</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Index Terms</head><item><term>Post-translational Modifications, Proteolysis & Proteomics</term></item><item><term>Metabolism</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2006-06-23">Received</change><change when="2006-12-05">Registration</change><change when="2007-02-07">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/A4EF349C681091C1E3681A33814CFCCCDBA85C97/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component type="serialArticle" version="2.0" xml:lang="en" xml:id="embj7601525"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Ltd</publisherName><publisherLoc>Chichester, UK</publisherLoc></publisherInfo><doi>10.1002/(ISSN)1460-2075</doi><issn type="print">0261-4189</issn><issn type="electronic">1460-2075</issn><idGroup><id type="product" value="EMBJ"></id></idGroup><titleGroup><title type="main" sort="THE EMBO JOURNAL">The EMBO Journal</title></titleGroup></publicationMeta><publicationMeta level="part" position="30"><doi>10.1002/emboj.v26.3</doi><copyright ownership="publisher">Copyright © 2013 Wiley Periodicals, Inc</copyright><numberingGroup><numbering type="journalVolume" number="26">26</numbering><numbering type="journalIssue">3</numbering></numberingGroup><coverDate startDate="2007-02-07">February 7, 2007</coverDate></publicationMeta><publicationMeta level="unit" position="200" type="article" status="forIssue"><doi>10.1038/sj.emboj.7601525</doi><idGroup><id type="unit" value="EMBJ7601525"></id></idGroup><countGroup><count type="pageTotal" number="11"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Article</title></titleGroup><copyright ownership="thirdParty">Copyright © 2007 European Molecular Biology Organization</copyright><eventGroup><event type="manuscriptReceived" date="2006-06-23"></event><event type="manuscriptAccepted" date="2006-12-05"></event><event type="publishedOnlineEarlyUnpaginated" date="2007-01-25"></event><event type="publishedOnlineFinalForm" date="2007-02-07"></event><event type="xmlConverted" agent="SPi Global Converter_TO_WileyML3Gv2.0 version:1.0; WileyML 3G Packaging Tool v1.0" date="2013-10-16"></event><event type="firstOnline" date="2007-01-25"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-04"></event></eventGroup><numberingGroup><numbering type="pageFirst">835</numbering><numbering type="pageLast">845</numbering></numberingGroup><correspondenceTo>Corresponding authors: IV Kurochkin, Genome Annotation and Comparative Analysis Team, Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, 1‐7‐22 Suehiro‐cho, Tsurumi‐ku, Yokohama, Kanagawa 230‐0045, Japan. Tel.: +81 45 503 9111 (ext 8106); Fax: +81 45 503 9176; E-mail: <email>igork@gsc.riken.jp</email> Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, 1397‐1 Yamane, Hidaka‐city, Saitama 350‐1241, Japan. Tel.: +81 42 985 7319; Fax: +81 42 985 7329; E-mail: <email>okazaki@saitama-med.ac.jp</email></correspondenceTo><subjectInfo><subject href="http://psi.embo.org/14602075/EMBO31">Post-translational Modifications, Proteolysis & Proteomics</subject><subject href="http://psi.embo.org/14602075/EMBO21">Metabolism</subject></subjectInfo><attributeValueGroup><attributeValue element="note" attribute="type" value="present-address"></attributeValue></attributeValueGroup><linkGroup><link type="toTypesetVersion" href="file:EMBJ.EMBJ7601525.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids</title><title type="short">Identification of peroxisomal processing protease</title></titleGroup><creators><creator creatorRole="author" xml:id="embj7601525-cr-0001" affiliationRef="#embj7601525-aff-0001" corresponding="yes"><personName><givenNames>Igor V</givenNames><familyName>Kurochkin</familyName></personName></creator><creator creatorRole="author" xml:id="embj7601525-cr-0002" affiliationRef="#embj7601525-aff-0002"><personName><givenNames>Yumi</givenNames><familyName>Mizuno</familyName></personName></creator><creator creatorRole="author" xml:id="embj7601525-cr-0003" affiliationRef="#embj7601525-aff-0003"><personName><givenNames>Akihiko</givenNames><familyName>Konagaya</familyName></personName></creator><creator creatorRole="author" xml:id="embj7601525-cr-0004" affiliationRef="#embj7601525-aff-0004"><personName><givenNames>Yoshiyuki</givenNames><familyName>Sakaki</familyName></personName></creator><creator creatorRole="author" xml:id="embj7601525-cr-0005" affiliationRef="#embj7601525-aff-0001" noteRef="#embj7601525-note-0002"><personName><givenNames>Christian</givenNames><familyName>Schönbach</familyName></personName></creator><creator creatorRole="author" xml:id="embj7601525-cr-0006" affiliationRef="#embj7601525-aff-0002" corresponding="yes"><personName><givenNames>Yasushi</givenNames><familyName>Okazaki</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="JP" type="organization" xml:id="embj7601525-aff-0001"><orgName>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center</orgName><address><city>Yokohama</city><country>Japan</country></address></affiliation><affiliation countryCode="JP" type="organization" xml:id="embj7601525-aff-0002"><orgName>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University</orgName><address><city>Hidaka‐shi</city><countryPart>Saitama</countryPart><country>Japan</country></address></affiliation><affiliation countryCode="JP" type="organization" xml:id="embj7601525-aff-0003"><orgName>RIKEN Genomic Sciences Center</orgName><address><city>Yokohama</city><country>Japan</country></address></affiliation><affiliation countryCode="JP" type="organization" xml:id="embj7601525-aff-0004"><orgName>Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center</orgName><address><city>Yokohama</city><country>Japan</country></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="embj7601525-kwd-0001">fatty acid oxidation</keyword><keyword xml:id="embj7601525-kwd-0002">peroxisomes</keyword><keyword xml:id="embj7601525-kwd-0003">protease</keyword><keyword xml:id="embj7601525-kwd-0004">protein processing</keyword><keyword xml:id="embj7601525-kwd-0005">Tysnd1</keyword></keywordGroup><supportingInformation><supportingInfoItem xml:id="embj7601525-sup-0001"><mediaResource alt="supplementary data" mimeType="application/pdf" href="urn-x:wiley:02614189:media:embj7601525:embj7601525-sup-0001"></mediaResource><caption><p>Supplementary data and Figure S1</p></caption></supportingInfoItem></supportingInformation><abstractGroup><abstract type="main"><p>Peroxisomes play an important role in β‐oxidation of fatty acids. All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1‐mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of β‐oxidation.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="embj7601525-note-0001" type="present-address">Present address: Genome Annotation and Comparative Analysis Team, Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, Yokohama 230‐0045, Japan</note><note xml:id="embj7601525-note-0002" type="present-address">Present address: Division of Genomics and Genetics, School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore</note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids</title></titleInfo><titleInfo type="abbreviated"><title>Identification of peroxisomal processing protease</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Novel peroxisomal protease Tysnd1 processes PTS1‐ and PTS2‐containing enzymes involved in β‐oxidation of fatty acids</title></titleInfo><name type="personal"><namePart type="given">Igor V</namePart><namePart type="family">Kurochkin</namePart><affiliation>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation><description>Correspondence: Corresponding authors: IV Kurochkin, Genome Annotation and Comparative Analysis Team, Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, 1‐7‐22 Suehiro‐cho, Tsurumi‐ku, Yokohama, Kanagawa 230‐0045, Japan. Tel.: +81 45 503 9111 (ext 8106); Fax: +81 45 503 9176; E-mail: Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, 1397‐1 Yamane, Hidaka‐city, Saitama 350‐1241, Japan. Tel.: +81 42 985 7319; Fax: +81 42 985 7329; E-mail: </description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yumi</namePart><namePart type="family">Mizuno</namePart><affiliation>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Akihiko</namePart><namePart type="family">Konagaya</namePart><affiliation>RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yoshiyuki</namePart><namePart type="family">Sakaki</namePart><affiliation>Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christian</namePart><namePart type="family">Schönbach</namePart><affiliation>Immunoinformatics Team, Advanced Genome Information Group, RIKEN Genomic Sciences Center, Yokohama, Japan</affiliation><description>Present address: Division of Genomics and Genetics, School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yasushi</namePart><namePart type="family">Okazaki</namePart><affiliation>Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, Saitama, Hidaka‐shi, Japan</affiliation><description>Correspondence: Corresponding authors: IV Kurochkin, Genome Annotation and Comparative Analysis Team, Computational and Experimental Systems Biology Group, RIKEN Genomic Sciences Center, 1‐7‐22 Suehiro‐cho, Tsurumi‐ku, Yokohama, Kanagawa 230‐0045, Japan. Tel.: +81 45 503 9111 (ext 8106); Fax: +81 45 503 9176; E-mail: Division of Functional Genomics and Systems Medicine, Research Center for Genomic Medicine, Saitama Medical University, 1397‐1 Yamane, Hidaka‐city, Saitama 350‐1241, Japan. Tel.: +81 42 985 7319; Fax: +81 42 985 7329; E-mail: </description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>John Wiley & Sons, Ltd</publisher><place><placeTerm type="text">Chichester, UK</placeTerm></place><dateIssued encoding="w3cdtf">2007-02-07</dateIssued><dateCaptured encoding="w3cdtf">2006-06-23</dateCaptured><dateValid encoding="w3cdtf">2006-12-05</dateValid><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract>Peroxisomes play an important role in β‐oxidation of fatty acids. All peroxisomal matrix proteins are synthesized in the cytosol and post‐translationally sorted to the organelle. Two distinct peroxisomal signal targeting sequences (PTSs), the C‐terminal PTS1 and the N‐terminal PTS2, have been defined. Import of precursor PTS2 proteins into the peroxisomes is accompanied by a proteolytic removal of the N‐terminal targeting sequence. Although the PTS1 signal is preserved upon translocation, many PTS1 proteins undergo a highly selective and limited cleavage. Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β‐oxidation. Tysnd1 itself undergoes processing through the removal of the presumably inhibitory N‐terminal fragment. Tysnd1 expression is induced by the proliferator‐activated receptor α agonist bezafibrate, along with the increase in its substrates. A model is proposed where the Tysnd1‐mediated processing of the peroxisomal enzymes promotes their assembly into a supramolecular complex to enhance the rate of β‐oxidation.</abstract><note type="additional physical form">Supplementary data and Figure S1</note><subject><genre>Keywords</genre><topic>fatty acid oxidation</topic><topic>peroxisomes</topic><topic>protease</topic><topic>protein processing</topic><topic>Tysnd1</topic></subject><relatedItem type="host"><titleInfo><title>The EMBO Journal</title></titleInfo><genre type="Journal">journal</genre><subject><genre>Index Terms</genre><topic authorityURI="http://psi.embo.org/14602075/EMBO31">Post-translational Modifications, Proteolysis & Proteomics</topic><topic authorityURI="http://psi.embo.org/14602075/EMBO21">Metabolism</topic></subject><subject><genre>article category</genre><topic>Article</topic></subject><identifier type="ISSN">0261-4189</identifier><identifier type="eISSN">1460-2075</identifier><identifier type="DOI">10.1002/(ISSN)1460-2075</identifier><identifier type="PublisherID">EMBJ</identifier><part><date>2007</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>835</start><end>845</end><total>11</total></extent></part></relatedItem><identifier type="istex">A4EF349C681091C1E3681A33814CFCCCDBA85C97</identifier><identifier type="DOI">10.1038/sj.emboj.7601525</identifier><identifier type="ArticleID">EMBJ7601525</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2013 Wiley Periodicals, IncCopyright © 2007 European Molecular Biology Organization</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>John Wiley & Sons, Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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