Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce.
Identifieur interne : 003356 ( Main/Exploration ); précédent : 003355; suivant : 003357Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce.
Auteurs : Kurt V. Fagerstedt [Finlande] ; Eija M. Kukkola ; Ville V T. Koistinen ; Junko Takahashi ; Kaisa MarjamaaSource :
- Journal of integrative plant biology [ 1744-7909 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- biosynthèse : Lignine.
- enzymologie : Picea.
- métabolisme : Lignine, Paroi cellulaire, Peroxidases, Picea.
English descriptors
- KwdEn :
- MESH :
Abstract
Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT-)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.
DOI: 10.1111/j.1744-7909.2010.00928.x
PubMed: 20377680
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kukkola</name></author><author><name sortKey="Koistinen, Ville V T" sort="Koistinen, Ville V T" uniqKey="Koistinen V" first="Ville V T" last="Koistinen">Ville V T. Koistinen</name></author><author><name sortKey="Takahashi, Junko" sort="Takahashi, Junko" uniqKey="Takahashi J" first="Junko" last="Takahashi">Junko Takahashi</name></author><author><name sortKey="Marjamaa, Kaisa" sort="Marjamaa, Kaisa" uniqKey="Marjamaa K" first="Kaisa" last="Marjamaa">Kaisa Marjamaa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20377680</idno><idno type="pmid">20377680</idno><idno type="doi">10.1111/j.1744-7909.2010.00928.x</idno><idno type="wicri:Area/Main/Corpus">003237</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003237</idno><idno type="wicri:Area/Main/Curation">003237</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003237</idno><idno type="wicri:Area/Main/Exploration">003237</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce.</title><author><name sortKey="Fagerstedt, Kurt V" sort="Fagerstedt, Kurt V" uniqKey="Fagerstedt K" first="Kurt V" last="Fagerstedt">Kurt V. 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Koistinen</name></author><author><name sortKey="Takahashi, Junko" sort="Takahashi, Junko" uniqKey="Takahashi J" first="Junko" last="Takahashi">Junko Takahashi</name></author><author><name sortKey="Marjamaa, Kaisa" sort="Marjamaa, Kaisa" uniqKey="Marjamaa K" first="Kaisa" last="Marjamaa">Kaisa Marjamaa</name></author></analytic><series><title level="j">Journal of integrative plant biology</title><idno type="eISSN">1744-7909</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Wall (metabolism)</term><term>Lignin (biosynthesis)</term><term>Lignin (metabolism)</term><term>Peroxidases (metabolism)</term><term>Picea (enzymology)</term><term>Picea (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Lignine (biosynthèse)</term><term>Lignine (métabolisme)</term><term>Paroi cellulaire (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Picea (enzymologie)</term><term>Picea (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Picea</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Picea</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Wall</term><term>Lignin</term><term>Peroxidases</term><term>Picea</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Paroi cellulaire</term><term>Peroxidases</term><term>Picea</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT-)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20377680</PMID><DateCompleted><Year>2010</Year><Month>07</Month><Day>08</Day></DateCompleted><DateRevised><Year>2010</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1744-7909</ISSN><JournalIssue CitedMedium="Internet"><Volume>52</Volume><Issue>2</Issue><PubDate><Year>2010</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of integrative plant biology</Title><ISOAbbreviation>J Integr Plant Biol</ISOAbbreviation></Journal><ArticleTitle>Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce.</ArticleTitle><Pagination><MedlinePgn>186-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1744-7909.2010.00928.x</ELocationID><Abstract><AbstractText>Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT-)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fagerstedt</LastName><ForeName>Kurt V</ForeName><Initials>KV</Initials><AffiliationInfo><Affiliation>Department of Biological and Environmental Sciences, Plant Biology, Helsinki University, Helsinki, Finland. kurt.fagerstedt@helsinki.fi</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kukkola</LastName><ForeName>Eija M</ForeName><Initials>EM</Initials></Author><Author ValidYN="Y"><LastName>Koistinen</LastName><ForeName>Ville V T</ForeName><Initials>VV</Initials></Author><Author ValidYN="Y"><LastName>Takahashi</LastName><ForeName>Junko</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Marjamaa</LastName><ForeName>Kaisa</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>China (Republic : 1949- )</Country><MedlineTA>J Integr Plant Biol</MedlineTA><NlmUniqueID>101250502</NlmUniqueID><ISSNLinking>1672-9072</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D028222" MajorTopicYN="N">Picea</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>83</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>4</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>4</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>7</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20377680</ArticleId><ArticleId IdType="pii">JIPB928</ArticleId><ArticleId IdType="doi">10.1111/j.1744-7909.2010.00928.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Finlande</li></country></list><tree><noCountry><name sortKey="Koistinen, Ville V T" sort="Koistinen, Ville V T" uniqKey="Koistinen V" first="Ville V T" last="Koistinen">Ville V T. Koistinen</name><name sortKey="Kukkola, Eija M" sort="Kukkola, Eija M" uniqKey="Kukkola E" first="Eija M" last="Kukkola">Eija M. Kukkola</name><name sortKey="Marjamaa, Kaisa" sort="Marjamaa, Kaisa" uniqKey="Marjamaa K" first="Kaisa" last="Marjamaa">Kaisa Marjamaa</name><name sortKey="Takahashi, Junko" sort="Takahashi, Junko" uniqKey="Takahashi J" first="Junko" last="Takahashi">Junko Takahashi</name></noCountry><country name="Finlande"><noRegion><name sortKey="Fagerstedt, Kurt V" sort="Fagerstedt, Kurt V" uniqKey="Fagerstedt K" first="Kurt V" last="Fagerstedt">Kurt V. Fagerstedt</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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