Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants.
Identifieur interne : 004829 ( Main/Corpus ); précédent : 004828; suivant : 004830Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants.
Auteurs : R. Zhong ; W H Morrison ; D S Himmelsbach ; F L Poole ; Z H YeSource :
- Plant physiology [ 0032-0889 ] ; 2000.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Cell Wall (chemistry), DNA Primers (genetics), Lignin (analysis), Lignin (biosynthesis), Methyltransferases (genetics), Methyltransferases (metabolism), Plant Stems (metabolism), Plants, Genetically Modified (MeSH), Spectroscopy, Fourier Transform Infrared (MeSH), Tissue Distribution (MeSH), Trees (genetics), Trees (growth & development), Trees (metabolism), Wood (MeSH).
- MESH :
- chemical , analysis : Lignin.
- chemical , biosynthesis : Lignin.
- chemical , genetics : DNA Primers, Methyltransferases.
- chemistry : Cell Wall.
- genetics : Trees.
- growth & development : Trees.
- chemical , metabolism : Methyltransferases, Plant Stems, Trees.
- Base Sequence, Plants, Genetically Modified, Spectroscopy, Fourier Transform Infrared, Tissue Distribution, Wood.
Abstract
Caffeoyl coenzyme A O-methyltransferase (CCoAOMT) has recently been shown to participate in lignin biosynthesis in herbacious tobacco plants. Here, we demonstrate that CCoAOMT is essential in lignin biosynthesis in woody poplar (Populus tremula x Populus alba) plants. In poplar stems, CCoAOMT was found to be expressed in all lignifying cells including vessel elements and fibers as well as in xylem ray parenchyma cells. Repression of CCoAOMT expression by the antisense approach in transgenic poplar plants caused a significant decrease in total lignin content as detected by both Klason lignin assay and Fourier-transform infrared spectroscopy. The reduction in lignin content was the result of a decrease in both guaiacyl and syringyl lignins as determined by in-source pyrolysis mass spectrometry. Fourier-transform infrared spectroscopy indicated that the reduction in lignin content resulted in a less condensed and less cross-linked lignin structure in wood. Repression of CCoAOMT expression also led to coloration of wood and an elevation of wall-bound p-hydroxybenzoic acid. Taken together, these results indicate that CCoAOMT plays a dominant role in the methylation of the 3-hydroxyl group of caffeoyl CoA, and the CCoAOMT-mediated methylation reaction is essential to channel substrates for 5-methoxylation of hydroxycinnamates. They also suggest that antisense repression of CCoAOMT is an efficient means for genetic engineering of trees with low lignin content.
DOI: 10.1104/pp.124.2.563
PubMed: 11027707
PubMed Central: PMC59163
Links to Exploration step
pubmed:11027707Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants.</title><author><name sortKey="Zhong, R" sort="Zhong, R" uniqKey="Zhong R" first="R" last="Zhong">R. Zhong</name><affiliation><nlm:affiliation>Department of Botany, University of Georgia, Athens, Georgia 30602, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Morrison, W H" sort="Morrison, W H" uniqKey="Morrison W" first="W H" last="Morrison">W H Morrison</name></author><author><name sortKey="Himmelsbach, D S" sort="Himmelsbach, D S" uniqKey="Himmelsbach D" first="D S" last="Himmelsbach">D S Himmelsbach</name></author><author><name sortKey="Poole, F L" sort="Poole, F L" uniqKey="Poole F" first="F L" last="Poole">F L Poole</name></author><author><name sortKey="Ye, Z H" sort="Ye, Z H" uniqKey="Ye Z" first="Z H" last="Ye">Z H Ye</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:11027707</idno><idno type="pmid">11027707</idno><idno type="pmc">PMC59163</idno><idno type="doi">10.1104/pp.124.2.563</idno><idno type="wicri:Area/Main/Corpus">004829</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004829</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants.</title><author><name sortKey="Zhong, R" sort="Zhong, R" uniqKey="Zhong R" first="R" last="Zhong">R. Zhong</name><affiliation><nlm:affiliation>Department of Botany, University of Georgia, Athens, Georgia 30602, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Morrison, W H" sort="Morrison, W H" uniqKey="Morrison W" first="W H" last="Morrison">W H Morrison</name></author><author><name sortKey="Himmelsbach, D S" sort="Himmelsbach, D S" uniqKey="Himmelsbach D" first="D S" last="Himmelsbach">D S Himmelsbach</name></author><author><name sortKey="Poole, F L" sort="Poole, F L" uniqKey="Poole F" first="F L" last="Poole">F L Poole</name></author><author><name sortKey="Ye, Z H" sort="Ye, Z H" uniqKey="Ye Z" first="Z H" last="Ye">Z H Ye</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Cell Wall (chemistry)</term><term>DNA Primers (genetics)</term><term>Lignin (analysis)</term><term>Lignin (biosynthesis)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (metabolism)</term><term>Plant Stems (metabolism)</term><term>Plants, Genetically Modified (MeSH)</term><term>Spectroscopy, Fourier Transform Infrared (MeSH)</term><term>Tissue Distribution (MeSH)</term><term>Trees (genetics)</term><term>Trees (growth & development)</term><term>Trees (metabolism)</term><term>Wood (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Wall</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Trees</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Trees</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Methyltransferases</term><term>Plant Stems</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Plants, Genetically Modified</term><term>Spectroscopy, Fourier Transform Infrared</term><term>Tissue Distribution</term><term>Wood</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Caffeoyl coenzyme A O-methyltransferase (CCoAOMT) has recently been shown to participate in lignin biosynthesis in herbacious tobacco plants. Here, we demonstrate that CCoAOMT is essential in lignin biosynthesis in woody poplar (Populus tremula x Populus alba) plants. In poplar stems, CCoAOMT was found to be expressed in all lignifying cells including vessel elements and fibers as well as in xylem ray parenchyma cells. Repression of CCoAOMT expression by the antisense approach in transgenic poplar plants caused a significant decrease in total lignin content as detected by both Klason lignin assay and Fourier-transform infrared spectroscopy. The reduction in lignin content was the result of a decrease in both guaiacyl and syringyl lignins as determined by in-source pyrolysis mass spectrometry. Fourier-transform infrared spectroscopy indicated that the reduction in lignin content resulted in a less condensed and less cross-linked lignin structure in wood. Repression of CCoAOMT expression also led to coloration of wood and an elevation of wall-bound p-hydroxybenzoic acid. Taken together, these results indicate that CCoAOMT plays a dominant role in the methylation of the 3-hydroxyl group of caffeoyl CoA, and the CCoAOMT-mediated methylation reaction is essential to channel substrates for 5-methoxylation of hydroxycinnamates. They also suggest that antisense repression of CCoAOMT is an efficient means for genetic engineering of trees with low lignin content.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11027707</PMID><DateCompleted><Year>2001</Year><Month>01</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>124</Volume><Issue>2</Issue><PubDate><Year>2000</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants.</ArticleTitle><Pagination><MedlinePgn>563-78</MedlinePgn></Pagination><Abstract><AbstractText>Caffeoyl coenzyme A O-methyltransferase (CCoAOMT) has recently been shown to participate in lignin biosynthesis in herbacious tobacco plants. Here, we demonstrate that CCoAOMT is essential in lignin biosynthesis in woody poplar (Populus tremula x Populus alba) plants. In poplar stems, CCoAOMT was found to be expressed in all lignifying cells including vessel elements and fibers as well as in xylem ray parenchyma cells. Repression of CCoAOMT expression by the antisense approach in transgenic poplar plants caused a significant decrease in total lignin content as detected by both Klason lignin assay and Fourier-transform infrared spectroscopy. The reduction in lignin content was the result of a decrease in both guaiacyl and syringyl lignins as determined by in-source pyrolysis mass spectrometry. Fourier-transform infrared spectroscopy indicated that the reduction in lignin content resulted in a less condensed and less cross-linked lignin structure in wood. Repression of CCoAOMT expression also led to coloration of wood and an elevation of wall-bound p-hydroxybenzoic acid. Taken together, these results indicate that CCoAOMT plays a dominant role in the methylation of the 3-hydroxyl group of caffeoyl CoA, and the CCoAOMT-mediated methylation reaction is essential to channel substrates for 5-methoxylation of hydroxycinnamates. They also suggest that antisense repression of CCoAOMT is an efficient means for genetic engineering of trees with low lignin content.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhong</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Botany, University of Georgia, Athens, Georgia 30602, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morrison</LastName><ForeName>W H</ForeName><Initials>WH</Initials><Suffix>3rd</Suffix></Author><Author ValidYN="Y"><LastName>Himmelsbach</LastName><ForeName>D S</ForeName><Initials>DS</Initials></Author><Author ValidYN="Y"><LastName>Poole</LastName><ForeName>F L</ForeName><Initials>FL</Initials><Suffix>2nd</Suffix></Author><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Z H</ForeName><Initials>ZH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.104</RegistryNumber><NameOfSubstance UI="C059825">caffeoyl-CoA O-methyltransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell 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