Differential expression of two distinct phenylalanine ammonia-lyase genes in condensed tannin-accumulating and lignifying cells of quaking aspen.
Identifieur interne : 004603 ( Main/Exploration ); précédent : 004602; suivant : 004604Differential expression of two distinct phenylalanine ammonia-lyase genes in condensed tannin-accumulating and lignifying cells of quaking aspen.
Auteurs : Yu-Ying Kao [États-Unis] ; Scott A. Harding ; Chung-Jui TsaiSource :
- Plant physiology [ 0032-0889 ] ; 2002.
Descripteurs français
- KwdFr :
- ADN complémentaire (composition chimique), ADN complémentaire (génétique), Acide salicylique (pharmacologie), Analyse de séquence d'ADN (MeSH), Contrainte mécanique (MeSH), Données de séquences moléculaires (MeSH), Hybridation in situ (MeSH), Lignine (métabolisme), Obscurité (MeSH), Phenylalanine ammonia-lyase (génétique), Phenylalanine ammonia-lyase (métabolisme), Phénols (métabolisme), Populus (cytologie), Populus (enzymologie), Populus (génétique), Protéines d'Arabidopsis (MeSH), Protéines végétales (génétique), Protéines végétales (métabolisme), Régulation de l'expression des gènes codant pour des enzymes (effets des médicaments et des substances chimiques), Régulation de l'expression des gènes végétaux (effets des médicaments et des substances chimiques), Serine endopeptidases (MeSH), Tanins hydrolysables (métabolisme), Technique de Northern (MeSH).
- MESH :
- composition chimique : ADN complémentaire.
- cytologie : Populus.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux.
- enzymologie : Populus.
- génétique : ADN complémentaire, Phenylalanine ammonia-lyase, Populus, Protéines végétales.
- métabolisme : Lignine, Phenylalanine ammonia-lyase, Phénols, Protéines végétales, Tanins hydrolysables.
- pharmacologie : Acide salicylique.
- Analyse de séquence d'ADN, Contrainte mécanique, Données de séquences moléculaires, Hybridation in situ, Obscurité, Protéines d'Arabidopsis, Serine endopeptidases, Technique de Northern.
English descriptors
- KwdEn :
- Arabidopsis Proteins (MeSH), Blotting, Northern (MeSH), DNA, Complementary (chemistry), DNA, Complementary (genetics), Darkness (MeSH), Gene Expression Regulation, Enzymologic (drug effects), Gene Expression Regulation, Plant (drug effects), Hydrolyzable Tannins (metabolism), In Situ Hybridization (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), Phenols (metabolism), Phenylalanine Ammonia-Lyase (genetics), Phenylalanine Ammonia-Lyase (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (cytology), Populus (enzymology), Populus (genetics), Salicylic Acid (pharmacology), Sequence Analysis, DNA (MeSH), Serine Endopeptidases (MeSH), Stress, Mechanical (MeSH).
- MESH :
- chemical , chemistry : DNA, Complementary.
- chemical , genetics : DNA, Complementary, Phenylalanine Ammonia-Lyase, Plant Proteins.
- chemical , metabolism : Hydrolyzable Tannins, Lignin, Phenols, Phenylalanine Ammonia-Lyase, Plant Proteins.
- chemical , pharmacology : Salicylic Acid.
- chemical : Arabidopsis Proteins, Serine Endopeptidases.
- cytology : Populus.
- drug effects : Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant.
- enzymology : Populus.
- genetics : Populus.
- Blotting, Northern, Darkness, In Situ Hybridization, Molecular Sequence Data, Sequence Analysis, DNA, Stress, Mechanical.
Abstract
Lignins, along with condensed tannins (CTs) and salicylate-derived phenolic glycosides, constitute potentially large phenylpropanoid carbon sinks in tissues of quaking aspen (Populus tremuloides Michx.). Metabolic commitment to each of these sinks varies during development and adaptation, and depends on L-phenylalanine ammonia-lyase (PAL), an enzyme catalyzing the deamination of L-phenylalanine to initiate phenylpropanoid metabolism. In Populus spp., PAL is encoded by multiple genes whose expression has been associated with lignification in primary and secondary tissues. We now report cloning two differentially expressed PAL cDNAs that exhibit distinct spatial associations with CT and lignin biosynthesis in developing shoot and root tissues of aspen. PtPAL1 was expressed in certain CT-accumulating, non-lignifying cells of stems, leaves, and roots, and the pattern of PtPAL1 expression varied coordinately with that of CT accumulation along the primary to secondary growth transition in stems. PtPAL2 was expressed in heavily lignified structural cells of shoots, but was also expressed in non-lignifying cells of root tips. Evidence of a role for Pt4CL2, encoding 4-coumarate:coenzyme A ligase, in determining CT sink strength was gained from cellular co-expression analysis with PAL1 and CTs, and from experiments in which leaf wounding increased PAL1 and 4CL2 expression as well as the relative allocation of carbon to CT with respect to phenolic glycoside, the dominant phenolic sink in aspen leaves. Leaf wounding also increased PAL2 and lignin pathway gene expression, but to a smaller extent. The absence of PAL2 in most CT-accumulating cells provides in situ support for the idea that PAL isoforms function in specific metabolic milieus.
DOI: 10.1104/pp.006262
PubMed: 12376645
PubMed Central: PMC166607
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Hybridization</term><term>Molecular Sequence Data</term><term>Sequence Analysis, DNA</term><term>Stress, Mechanical</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Contrainte mécanique</term><term>Données de séquences moléculaires</term><term>Hybridation in situ</term><term>Obscurité</term><term>Protéines d'Arabidopsis</term><term>Serine endopeptidases</term><term>Technique de Northern</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignins, along with condensed tannins (CTs) and salicylate-derived phenolic glycosides, constitute potentially large phenylpropanoid carbon sinks in tissues of quaking aspen (Populus tremuloides Michx.). Metabolic commitment to each of these sinks varies during development and adaptation, and depends on L-phenylalanine ammonia-lyase (PAL), an enzyme catalyzing the deamination of L-phenylalanine to initiate phenylpropanoid metabolism. In Populus spp., PAL is encoded by multiple genes whose expression has been associated with lignification in primary and secondary tissues. We now report cloning two differentially expressed PAL cDNAs that exhibit distinct spatial associations with CT and lignin biosynthesis in developing shoot and root tissues of aspen. PtPAL1 was expressed in certain CT-accumulating, non-lignifying cells of stems, leaves, and roots, and the pattern of PtPAL1 expression varied coordinately with that of CT accumulation along the primary to secondary growth transition in stems. PtPAL2 was expressed in heavily lignified structural cells of shoots, but was also expressed in non-lignifying cells of root tips. Evidence of a role for Pt4CL2, encoding 4-coumarate:coenzyme A ligase, in determining CT sink strength was gained from cellular co-expression analysis with PAL1 and CTs, and from experiments in which leaf wounding increased PAL1 and 4CL2 expression as well as the relative allocation of carbon to CT with respect to phenolic glycoside, the dominant phenolic sink in aspen leaves. Leaf wounding also increased PAL2 and lignin pathway gene expression, but to a smaller extent. The absence of PAL2 in most CT-accumulating cells provides in situ support for the idea that PAL isoforms function in specific metabolic milieus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12376645</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>130</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Differential expression of two distinct phenylalanine ammonia-lyase genes in condensed tannin-accumulating and lignifying cells of quaking aspen.</ArticleTitle><Pagination><MedlinePgn>796-807</MedlinePgn></Pagination><Abstract><AbstractText>Lignins, along with condensed tannins (CTs) and salicylate-derived phenolic glycosides, constitute potentially large phenylpropanoid carbon sinks in tissues of quaking aspen (Populus tremuloides Michx.). Metabolic commitment to each of these sinks varies during development and adaptation, and depends on L-phenylalanine ammonia-lyase (PAL), an enzyme catalyzing the deamination of L-phenylalanine to initiate phenylpropanoid metabolism. In Populus spp., PAL is encoded by multiple genes whose expression has been associated with lignification in primary and secondary tissues. We now report cloning two differentially expressed PAL cDNAs that exhibit distinct spatial associations with CT and lignin biosynthesis in developing shoot and root tissues of aspen. PtPAL1 was expressed in certain CT-accumulating, non-lignifying cells of stems, leaves, and roots, and the pattern of PtPAL1 expression varied coordinately with that of CT accumulation along the primary to secondary growth transition in stems. PtPAL2 was expressed in heavily lignified structural cells of shoots, but was also expressed in non-lignifying cells of root tips. Evidence of a role for Pt4CL2, encoding 4-coumarate:coenzyme A ligase, in determining CT sink strength was gained from cellular co-expression analysis with PAL1 and CTs, and from experiments in which leaf wounding increased PAL1 and 4CL2 expression as well as the relative allocation of carbon to CT with respect to phenolic glycoside, the dominant phenolic sink in aspen leaves. Leaf wounding also increased PAL2 and lignin pathway gene expression, but to a smaller extent. The absence of PAL2 in most CT-accumulating cells provides in situ support for the idea that PAL isoforms function in specific metabolic milieus.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kao</LastName><ForeName>Yu-Ying</ForeName><Initials>YY</Initials><AffiliationInfo><Affiliation>Plant Biotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton, MI 49931, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harding</LastName><ForeName>Scott A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Tsai</LastName><ForeName>Chung-Jui</ForeName><Initials>CJ</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AF480619</AccessionNumber></AccessionNumberList></DataBank></DataBankList><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="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047348">Hydrolyzable Tannins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><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 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.3.1.24</RegistryNumber><NameOfSubstance UI="D010650">Phenylalanine Ammonia-Lyase</NameOfSubstance></Chemical><Chemical><RegistryNumber>O414PZ4LPZ</RegistryNumber><NameOfSubstance UI="D020156">Salicylic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015152" MajorTopicYN="N">Blotting, Northern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003624" MajorTopicYN="N">Darkness</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D047348" MajorTopicYN="N">Hydrolyzable Tannins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017403" MajorTopicYN="N">In Situ Hybridization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010636" MajorTopicYN="N">Phenols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010650" MajorTopicYN="N">Phenylalanine Ammonia-Lyase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020156" MajorTopicYN="N">Salicylic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013314" MajorTopicYN="N">Stress, Mechanical</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>10</Month><Day>12</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>2</Month><Day>7</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">9887524</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region></list><tree><noCountry><name sortKey="Harding, Scott A" sort="Harding, Scott A" uniqKey="Harding S" first="Scott A" last="Harding">Scott A. Harding</name><name sortKey="Tsai, Chung Jui" sort="Tsai, Chung Jui" uniqKey="Tsai C" first="Chung-Jui" last="Tsai">Chung-Jui Tsai</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Kao, Yu Ying" sort="Kao, Yu Ying" uniqKey="Kao Y" first="Yu-Ying" last="Kao">Yu-Ying Kao</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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