Immunohistochemical localization of enzymes that catalyze the long sequential pathways of lignin biosynthesis during differentiation of secondary xylem tissues of hybrid aspen (Populus sieboldii x Populus grandidentata).
Identifieur interne : 003593 ( Main/Exploration ); précédent : 003592; suivant : 003594Immunohistochemical localization of enzymes that catalyze the long sequential pathways of lignin biosynthesis during differentiation of secondary xylem tissues of hybrid aspen (Populus sieboldii x Populus grandidentata).
Auteurs : Kanna Sato [Japon] ; Nobuyuki Nishikubo ; Yoko Mashino ; Kaori Yoshitomi ; Jinmei Zhou ; Shinya Kajita ; Yoshihiro KatayamaSource :
- Tree physiology [ 0829-318X ] ; 2009.
Descripteurs français
- KwdFr :
- 3-Deoxy-7-phosphoheptulonate synthase (analyse), 3-Deoxy-7-phosphoheptulonate synthase (métabolisme), 3-Deoxy-7-phosphoheptulonate synthase (physiologie), Alcohol oxidoreductases (analyse), Alcohol oxidoreductases (métabolisme), Alcohol oxidoreductases (physiologie), Coenzyme A ligases (analyse), Coenzyme A ligases (métabolisme), Coenzyme A ligases (physiologie), Glutamate-ammonia ligase (analyse), Glutamate-ammonia ligase (métabolisme), Glutamate-ammonia ligase (physiologie), Hybridation génétique (MeSH), Immunohistochimie (MeSH), Lignine (biosynthèse), Methyltransferases (analyse), Methyltransferases (métabolisme), Methyltransferases (physiologie), Phenylalanine ammonia-lyase (analyse), Phenylalanine ammonia-lyase (métabolisme), Phenylalanine ammonia-lyase (physiologie), Populus (enzymologie), Populus (génétique), Populus (métabolisme), Protéines végétales (analyse), Protéines végétales (métabolisme), Protéines végétales (physiologie), Xylème (croissance et développement), Xylème (enzymologie), Xylème (métabolisme).
- MESH :
- analyse : 3-Deoxy-7-phosphoheptulonate synthase, Alcohol oxidoreductases, Coenzyme A ligases, Glutamate-ammonia ligase, Methyltransferases, Phenylalanine ammonia-lyase, Protéines végétales.
- biosynthèse : Lignine.
- croissance et développement : Xylème.
- enzymologie : Populus, Xylème.
- génétique : Populus.
- métabolisme : 3-Deoxy-7-phosphoheptulonate synthase, Alcohol oxidoreductases, Coenzyme A ligases, Glutamate-ammonia ligase, Methyltransferases, Phenylalanine ammonia-lyase, Populus, Protéines végétales, Xylème.
- physiologie : 3-Deoxy-7-phosphoheptulonate synthase, Alcohol oxidoreductases, Coenzyme A ligases, Glutamate-ammonia ligase, Methyltransferases, Phenylalanine ammonia-lyase, Protéines végétales.
- Hybridation génétique, Immunohistochimie.
English descriptors
- KwdEn :
- 3-Deoxy-7-Phosphoheptulonate Synthase (analysis), 3-Deoxy-7-Phosphoheptulonate Synthase (metabolism), 3-Deoxy-7-Phosphoheptulonate Synthase (physiology), Alcohol Oxidoreductases (analysis), Alcohol Oxidoreductases (metabolism), Alcohol Oxidoreductases (physiology), Coenzyme A Ligases (analysis), Coenzyme A Ligases (metabolism), Coenzyme A Ligases (physiology), Glutamate-Ammonia Ligase (analysis), Glutamate-Ammonia Ligase (metabolism), Glutamate-Ammonia Ligase (physiology), Hybridization, Genetic (MeSH), Immunohistochemistry (MeSH), Lignin (biosynthesis), Methyltransferases (analysis), Methyltransferases (metabolism), Methyltransferases (physiology), Phenylalanine Ammonia-Lyase (analysis), Phenylalanine Ammonia-Lyase (metabolism), Phenylalanine Ammonia-Lyase (physiology), Plant Proteins (analysis), Plant Proteins (metabolism), Plant Proteins (physiology), Populus (enzymology), Populus (genetics), Populus (metabolism), Xylem (enzymology), Xylem (growth & development), Xylem (metabolism).
- MESH :
- chemical , analysis : 3-Deoxy-7-Phosphoheptulonate Synthase, Alcohol Oxidoreductases, Coenzyme A Ligases, Glutamate-Ammonia Ligase, Methyltransferases, Phenylalanine Ammonia-Lyase, Plant Proteins.
- chemical , biosynthesis : Lignin.
- chemical , metabolism : 3-Deoxy-7-Phosphoheptulonate Synthase, Alcohol Oxidoreductases, Coenzyme A Ligases, Glutamate-Ammonia Ligase, Methyltransferases, Phenylalanine Ammonia-Lyase, Plant Proteins.
- chemical , physiology : 3-Deoxy-7-Phosphoheptulonate Synthase, Alcohol Oxidoreductases, Coenzyme A Ligases, Glutamate-Ammonia Ligase, Methyltransferases, Phenylalanine Ammonia-Lyase, Plant Proteins.
- enzymology : Populus, Xylem.
- genetics : Populus.
- growth & development : Xylem.
- metabolism : Populus, Xylem.
- Hybridization, Genetic, Immunohistochemistry.
Abstract
We have investigated the spatial localization of enzymes that catalyze the sequential pathways of lignin biosynthesis in developing secondary xylem tissues of hybrid aspen (Populus sieboldii Miq. x Populus grandidentata Michx.) using immunohistochemical techniques. The enzymes phenylalanine ammonia-lyase, caffeic acid 3-O-methyltransferase and 4-coumarate:CoA ligase in the common phenylpropanoid pathway, cinnamyl-alcohol dehydrogenase (CAD) and peroxidase in the specific lignin pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) in the shikimate pathway and glutamine synthetase (GS) in the nitrogen reassimilation system were abundantly localized in the 6th to 9th wood fibers away from cambium; these wood fibers are likely undergoing the most intense lignification. Only weak immunolabeling of enzymes involved in the general phenylpropanoid and specific lignin pathways was detected in the cells near the cambium; lignification of these cells has likely been initiated after primary cell wall formation. In contrast, distinct localization of DAHPS and GS was observed around the cambium, which may be involved not only in lignin biosynthesis, but also in amino acid and protein synthesis, which are essential for cell survival. Our observations suggest that co-localization of enzymes related to the sequential shikimate, general phenylpropanoid and specific lignin branch pathways and to the nitrogen recycling system is associated with cell wall lignification of wood fibers during secondary xylem development.
DOI: 10.1093/treephys/tpp069
PubMed: 19910325
Affiliations:
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uniqKey="Nishikubo N" first="Nobuyuki" last="Nishikubo">Nobuyuki Nishikubo</name></author><author><name sortKey="Mashino, Yoko" sort="Mashino, Yoko" uniqKey="Mashino Y" first="Yoko" last="Mashino">Yoko Mashino</name></author><author><name sortKey="Yoshitomi, Kaori" sort="Yoshitomi, Kaori" uniqKey="Yoshitomi K" first="Kaori" last="Yoshitomi">Kaori Yoshitomi</name></author><author><name sortKey="Zhou, Jinmei" sort="Zhou, Jinmei" uniqKey="Zhou J" first="Jinmei" last="Zhou">Jinmei Zhou</name></author><author><name sortKey="Kajita, Shinya" sort="Kajita, Shinya" uniqKey="Kajita S" first="Shinya" last="Kajita">Shinya Kajita</name></author><author><name sortKey="Katayama, Yoshihiro" sort="Katayama, Yoshihiro" uniqKey="Katayama Y" first="Yoshihiro" last="Katayama">Yoshihiro Katayama</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19910325</idno><idno type="pmid">19910325</idno><idno 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last="Kajita">Shinya Kajita</name></author><author><name sortKey="Katayama, Yoshihiro" sort="Katayama, Yoshihiro" uniqKey="Katayama Y" first="Yoshihiro" last="Katayama">Yoshihiro Katayama</name></author></analytic><series><title level="j">Tree physiology</title><idno type="ISSN">0829-318X</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3-Deoxy-7-Phosphoheptulonate Synthase (analysis)</term><term>3-Deoxy-7-Phosphoheptulonate Synthase (metabolism)</term><term>3-Deoxy-7-Phosphoheptulonate Synthase (physiology)</term><term>Alcohol Oxidoreductases (analysis)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Alcohol Oxidoreductases (physiology)</term><term>Coenzyme A Ligases (analysis)</term><term>Coenzyme A Ligases (metabolism)</term><term>Coenzyme A Ligases (physiology)</term><term>Glutamate-Ammonia Ligase (analysis)</term><term>Glutamate-Ammonia Ligase (metabolism)</term><term>Glutamate-Ammonia Ligase (physiology)</term><term>Hybridization, Genetic (MeSH)</term><term>Immunohistochemistry (MeSH)</term><term>Lignin (biosynthesis)</term><term>Methyltransferases (analysis)</term><term>Methyltransferases (metabolism)</term><term>Methyltransferases (physiology)</term><term>Phenylalanine Ammonia-Lyase (analysis)</term><term>Phenylalanine Ammonia-Lyase (metabolism)</term><term>Phenylalanine Ammonia-Lyase (physiology)</term><term>Plant Proteins (analysis)</term><term>Plant Proteins (metabolism)</term><term>Plant Proteins (physiology)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Populus (metabolism)</term><term>Xylem (enzymology)</term><term>Xylem (growth & development)</term><term>Xylem (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>3-Deoxy-7-phosphoheptulonate synthase (analyse)</term><term>3-Deoxy-7-phosphoheptulonate synthase (métabolisme)</term><term>3-Deoxy-7-phosphoheptulonate synthase (physiologie)</term><term>Alcohol oxidoreductases (analyse)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Alcohol oxidoreductases (physiologie)</term><term>Coenzyme A ligases (analyse)</term><term>Coenzyme A ligases (métabolisme)</term><term>Coenzyme A ligases (physiologie)</term><term>Glutamate-ammonia ligase (analyse)</term><term>Glutamate-ammonia ligase (métabolisme)</term><term>Glutamate-ammonia ligase (physiologie)</term><term>Hybridation génétique (MeSH)</term><term>Immunohistochimie (MeSH)</term><term>Lignine (biosynthèse)</term><term>Methyltransferases (analyse)</term><term>Methyltransferases (métabolisme)</term><term>Methyltransferases (physiologie)</term><term>Phenylalanine ammonia-lyase (analyse)</term><term>Phenylalanine ammonia-lyase (métabolisme)</term><term>Phenylalanine ammonia-lyase (physiologie)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Populus (métabolisme)</term><term>Protéines végétales (analyse)</term><term>Protéines végétales (métabolisme)</term><term>Protéines végétales (physiologie)</term><term>Xylème (croissance et développement)</term><term>Xylème (enzymologie)</term><term>Xylème (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>3-Deoxy-7-Phosphoheptulonate Synthase</term><term>Alcohol Oxidoreductases</term><term>Coenzyme A Ligases</term><term>Glutamate-Ammonia Ligase</term><term>Methyltransferases</term><term>Phenylalanine Ammonia-Lyase</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>3-Deoxy-7-Phosphoheptulonate Synthase</term><term>Alcohol Oxidoreductases</term><term>Coenzyme A Ligases</term><term>Glutamate-Ammonia Ligase</term><term>Methyltransferases</term><term>Phenylalanine Ammonia-Lyase</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>3-Deoxy-7-Phosphoheptulonate Synthase</term><term>Alcohol Oxidoreductases</term><term>Coenzyme A Ligases</term><term>Glutamate-Ammonia Ligase</term><term>Methyltransferases</term><term>Phenylalanine Ammonia-Lyase</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>3-Deoxy-7-phosphoheptulonate synthase</term><term>Alcohol oxidoreductases</term><term>Coenzyme A ligases</term><term>Glutamate-ammonia ligase</term><term>Methyltransferases</term><term>Phenylalanine ammonia-lyase</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Xylème</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term><term>Xylème</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term><term>Xylem</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Xylem</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term><term>Xylem</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>3-Deoxy-7-phosphoheptulonate synthase</term><term>Alcohol oxidoreductases</term><term>Coenzyme A ligases</term><term>Glutamate-ammonia ligase</term><term>Methyltransferases</term><term>Phenylalanine ammonia-lyase</term><term>Populus</term><term>Protéines végétales</term><term>Xylème</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>3-Deoxy-7-phosphoheptulonate synthase</term><term>Alcohol oxidoreductases</term><term>Coenzyme A ligases</term><term>Glutamate-ammonia ligase</term><term>Methyltransferases</term><term>Phenylalanine ammonia-lyase</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hybridization, Genetic</term><term>Immunohistochemistry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Hybridation génétique</term><term>Immunohistochimie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have investigated the spatial localization of enzymes that catalyze the sequential pathways of lignin biosynthesis in developing secondary xylem tissues of hybrid aspen (Populus sieboldii Miq. x Populus grandidentata Michx.) using immunohistochemical techniques. The enzymes phenylalanine ammonia-lyase, caffeic acid 3-O-methyltransferase and 4-coumarate:CoA ligase in the common phenylpropanoid pathway, cinnamyl-alcohol dehydrogenase (CAD) and peroxidase in the specific lignin pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) in the shikimate pathway and glutamine synthetase (GS) in the nitrogen reassimilation system were abundantly localized in the 6th to 9th wood fibers away from cambium; these wood fibers are likely undergoing the most intense lignification. Only weak immunolabeling of enzymes involved in the general phenylpropanoid and specific lignin pathways was detected in the cells near the cambium; lignification of these cells has likely been initiated after primary cell wall formation. In contrast, distinct localization of DAHPS and GS was observed around the cambium, which may be involved not only in lignin biosynthesis, but also in amino acid and protein synthesis, which are essential for cell survival. Our observations suggest that co-localization of enzymes related to the sequential shikimate, general phenylpropanoid and specific lignin branch pathways and to the nitrogen recycling system is associated with cell wall lignification of wood fibers during secondary xylem development.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19910325</PMID><DateCompleted><Year>2010</Year><Month>02</Month><Day>23</Day></DateCompleted><DateRevised><Year>2009</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0829-318X</ISSN><JournalIssue CitedMedium="Print"><Volume>29</Volume><Issue>12</Issue><PubDate><Year>2009</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Tree physiology</Title><ISOAbbreviation>Tree Physiol</ISOAbbreviation></Journal><ArticleTitle>Immunohistochemical localization of enzymes that catalyze the long sequential pathways of lignin biosynthesis during differentiation of secondary xylem tissues of hybrid aspen (Populus sieboldii x Populus grandidentata).</ArticleTitle><Pagination><MedlinePgn>1599-606</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/treephys/tpp069</ELocationID><Abstract><AbstractText>We have investigated the spatial localization of enzymes that catalyze the sequential pathways of lignin biosynthesis in developing secondary xylem tissues of hybrid aspen (Populus sieboldii Miq. x Populus grandidentata Michx.) using immunohistochemical techniques. The enzymes phenylalanine ammonia-lyase, caffeic acid 3-O-methyltransferase and 4-coumarate:CoA ligase in the common phenylpropanoid pathway, cinnamyl-alcohol dehydrogenase (CAD) and peroxidase in the specific lignin pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) in the shikimate pathway and glutamine synthetase (GS) in the nitrogen reassimilation system were abundantly localized in the 6th to 9th wood fibers away from cambium; these wood fibers are likely undergoing the most intense lignification. Only weak immunolabeling of enzymes involved in the general phenylpropanoid and specific lignin pathways was detected in the cells near the cambium; lignification of these cells has likely been initiated after primary cell wall formation. In contrast, distinct localization of DAHPS and GS was observed around the cambium, which may be involved not only in lignin biosynthesis, but also in amino acid and protein synthesis, which are essential for cell survival. Our observations suggest that co-localization of enzymes related to the sequential shikimate, general phenylpropanoid and specific lignin branch pathways and to the nitrogen recycling system is associated with cell wall lignification of wood fibers during secondary xylem development.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Kanna</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nishikubo</LastName><ForeName>Nobuyuki</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Mashino</LastName><ForeName>Yoko</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Yoshitomi</LastName><ForeName>Kaori</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Jinmei</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kajita</LastName><ForeName>Shinya</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Katayama</LastName><ForeName>Yoshihiro</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Canada</Country><MedlineTA>Tree Physiol</MedlineTA><NlmUniqueID>100955338</NlmUniqueID><ISSNLinking>0829-318X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.195</RegistryNumber><NameOfSubstance UI="C018656">cinnamyl alcohol dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.68</RegistryNumber><NameOfSubstance UI="C019608">caffeate O-methyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.54</RegistryNumber><NameOfSubstance UI="D010723">3-Deoxy-7-Phosphoheptulonate Synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.3.1.24</RegistryNumber><NameOfSubstance UI="D010650">Phenylalanine Ammonia-Lyase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.2.1.-</RegistryNumber><NameOfSubstance UI="D003066">Coenzyme A Ligases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.2.1.12</RegistryNumber><NameOfSubstance UI="C019943">4-coumarate-CoA ligase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.1.2</RegistryNumber><NameOfSubstance UI="D005974">Glutamate-Ammonia Ligase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D010723" MajorTopicYN="N">3-Deoxy-7-Phosphoheptulonate Synthase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003066" MajorTopicYN="N">Coenzyme A Ligases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005974" MajorTopicYN="N">Glutamate-Ammonia Ligase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006824" MajorTopicYN="N">Hybridization, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010650" MajorTopicYN="N">Phenylalanine Ammonia-Lyase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D052584" MajorTopicYN="N">Xylem</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>11</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>11</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>2</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19910325</ArticleId><ArticleId IdType="pii">tpp069</ArticleId><ArticleId IdType="doi">10.1093/treephys/tpp069</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Kajita, Shinya" sort="Kajita, Shinya" uniqKey="Kajita S" first="Shinya" last="Kajita">Shinya Kajita</name><name sortKey="Katayama, Yoshihiro" sort="Katayama, Yoshihiro" uniqKey="Katayama Y" first="Yoshihiro" last="Katayama">Yoshihiro Katayama</name><name sortKey="Mashino, Yoko" sort="Mashino, Yoko" uniqKey="Mashino Y" first="Yoko" last="Mashino">Yoko Mashino</name><name sortKey="Nishikubo, Nobuyuki" sort="Nishikubo, Nobuyuki" uniqKey="Nishikubo N" first="Nobuyuki" last="Nishikubo">Nobuyuki Nishikubo</name><name sortKey="Yoshitomi, Kaori" sort="Yoshitomi, Kaori" uniqKey="Yoshitomi K" first="Kaori" last="Yoshitomi">Kaori Yoshitomi</name><name sortKey="Zhou, Jinmei" sort="Zhou, Jinmei" uniqKey="Zhou J" first="Jinmei" last="Zhou">Jinmei Zhou</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Sato, Kanna" sort="Sato, Kanna" uniqKey="Sato K" first="Kanna" last="Sato">Kanna Sato</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Immunohistochemical localization of enzymes that catalyze the long sequential pathways of lignin biosynthesis during differentiation of secondary xylem tissues of hybrid aspen (Populus sieboldii x Populus grandidentata).
}}
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