Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.
Identifieur interne : 002518 ( Main/Exploration ); précédent : 002517; suivant : 002519Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.
Auteurs : Jun Shigeto [Japon] ; Yuko Kiyonaga ; Koki Fujita ; Ryuichiro Kondo ; Yuji TsutsumiSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2013.
Descripteurs français
- KwdFr :
- Arabidopsis (enzymologie), Cations (MeSH), Isoenzymes (métabolisme), Lignine (biosynthèse), Oxydoréduction (MeSH), Paroi cellulaire (enzymologie), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Protéines d'Arabidopsis (composition chimique), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Tyrosine (composition chimique).
- MESH :
- biosynthèse : Lignine.
- composition chimique : Peroxidases, Protéines d'Arabidopsis, Tyrosine.
- enzymologie : Arabidopsis, Paroi cellulaire.
- génétique : Peroxidases, Protéines d'Arabidopsis.
- métabolisme : Isoenzymes, Peroxidases, Protéines d'Arabidopsis.
- Cations, Oxydoréduction.
English descriptors
- KwdEn :
- Arabidopsis (enzymology), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Cations (MeSH), Cell Wall (enzymology), Isoenzymes (metabolism), Lignin (biosynthesis), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Tyrosine (chemistry).
- MESH :
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Arabidopsis Proteins, Peroxidases, Tyrosine.
- enzymology : Arabidopsis, Cell Wall.
- chemical , genetics : Arabidopsis Proteins, Peroxidases.
- chemical , metabolism : Arabidopsis Proteins, Isoenzymes, Peroxidases.
- chemical : Cations, Oxidation-Reduction.
Abstract
The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls.
DOI: 10.1021/jf400426g
PubMed: 23551275
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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last="Fujita">Koki Fujita</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23551275</idno><idno type="pmid">23551275</idno><idno type="doi">10.1021/jf400426g</idno><idno type="wicri:Area/Main/Corpus">002645</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002645</idno><idno type="wicri:Area/Main/Curation">002645</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002645</idno><idno type="wicri:Area/Main/Exploration">002645</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.</title><author><name sortKey="Shigeto, Jun" sort="Shigeto, Jun" uniqKey="Shigeto J" first="Jun" last="Shigeto">Jun Shigeto</name><affiliation wicri:level="1"><nlm:affiliation>Department of Forest and Forest Products Sciences, Kyushu University , 6-10-1 Hakozaki, Higashi-ku, Fukuoka, 812-8581 Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Forest and Forest Products Sciences, Kyushu University , 6-10-1 Hakozaki, Higashi-ku, Fukuoka</wicri:regionArea><wicri:noRegion>Fukuoka</wicri:noRegion></affiliation></author><author><name sortKey="Kiyonaga, Yuko" sort="Kiyonaga, Yuko" uniqKey="Kiyonaga Y" first="Yuko" last="Kiyonaga">Yuko Kiyonaga</name></author><author><name sortKey="Fujita, Koki" sort="Fujita, Koki" uniqKey="Fujita K" first="Koki" last="Fujita">Koki Fujita</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author></analytic><series><title level="j">Journal of agricultural and food chemistry</title><idno type="eISSN">1520-5118</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (enzymology)</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (genetics)</term><term>Arabidopsis Proteins (metabolism)</term><term>Cations (MeSH)</term><term>Cell Wall (enzymology)</term><term>Isoenzymes (metabolism)</term><term>Lignin (biosynthesis)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Tyrosine (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (enzymologie)</term><term>Cations (MeSH)</term><term>Isoenzymes (métabolisme)</term><term>Lignine (biosynthèse)</term><term>Oxydoréduction (MeSH)</term><term>Paroi cellulaire (enzymologie)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Protéines d'Arabidopsis (composition chimique)</term><term>Protéines d'Arabidopsis (génétique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Tyrosine (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>Peroxidases</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term><term>Protéines d'Arabidopsis</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term><term>Paroi cellulaire</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term><term>Cell Wall</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Protéines d'Arabidopsis</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isoenzymes</term><term>Peroxidases</term><term>Protéines d'Arabidopsis</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cations</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23551275</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>30</Day></DateCompleted><DateRevised><Year>2015</Year><Month>06</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5118</ISSN><JournalIssue CitedMedium="Internet"><Volume>61</Volume><Issue>16</Issue><PubDate><Year>2013</Year><Month>Apr</Month><Day>24</Day></PubDate></JournalIssue><Title>Journal of agricultural and food chemistry</Title><ISOAbbreviation>J Agric Food Chem</ISOAbbreviation></Journal><ArticleTitle>Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.</ArticleTitle><Pagination><MedlinePgn>3781-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jf400426g</ELocationID><Abstract><AbstractText>The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shigeto</LastName><ForeName>Jun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Forest and Forest Products Sciences, Kyushu University , 6-10-1 Hakozaki, Higashi-ku, Fukuoka, 812-8581 Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kiyonaga</LastName><ForeName>Yuko</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Fujita</LastName><ForeName>Koki</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Kondo</LastName><ForeName>Ryuichiro</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Tsutsumi</LastName><ForeName>Yuji</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>04</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Agric Food Chem</MedlineTA><NlmUniqueID>0374755</NlmUniqueID><ISSNLinking>0021-8561</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>7</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23551275</ArticleId><ArticleId IdType="doi">10.1021/jf400426g</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Fujita, Koki" sort="Fujita, Koki" uniqKey="Fujita K" first="Koki" last="Fujita">Koki Fujita</name><name sortKey="Kiyonaga, Yuko" sort="Kiyonaga, Yuko" uniqKey="Kiyonaga Y" first="Yuko" last="Kiyonaga">Yuko Kiyonaga</name><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></noCountry><country name="Japon"><noRegion><name sortKey="Shigeto, Jun" sort="Shigeto, Jun" uniqKey="Shigeto J" first="Jun" last="Shigeto">Jun Shigeto</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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