Differential substrate inhibition couples kinetically distinct 4-coumarate:coenzyme a ligases with spatially distinct metabolic roles in quaking aspen.
Identifieur interne : 004602 ( Main/Exploration ); précédent : 004601; suivant : 004603Differential substrate inhibition couples kinetically distinct 4-coumarate:coenzyme a ligases with spatially distinct metabolic roles in quaking aspen.
Auteurs : Scott A. Harding [États-Unis] ; Jacqueline Leshkevich ; Vincent L. Chiang ; Chung-Jui TsaiSource :
- Plant physiology [ 0032-0889 ] ; 2002.
Descripteurs français
- KwdFr :
- Acides caféiques (métabolisme), Acides coumariques (métabolisme), Acyl coenzyme A (métabolisme), Cinétique (MeSH), Clonage moléculaire (MeSH), Coenzyme A ligases (génétique), Coenzyme A ligases (métabolisme), Flavonoïdes (biosynthèse), Flavonoïdes (composition chimique), Hybridation in situ (MeSH), Isoenzymes (génétique), Isoenzymes (métabolisme), Lignine (biosynthèse), Lignine (composition chimique), Pinus (enzymologie), Pinus (génétique), Protéines recombinantes (métabolisme), Régions promotrices (génétique) (MeSH), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Salicaceae (enzymologie), Salicaceae (génétique), Tiges de plante (cytologie), Tiges de plante (enzymologie), Tiges de plante (génétique).
- MESH :
- biosynthèse : Flavonoïdes, Lignine.
- composition chimique : Flavonoïdes, Lignine.
- cytologie : Tiges de plante.
- enzymologie : Pinus, Salicaceae, Tiges de plante.
- génétique : Coenzyme A ligases, Isoenzymes, Pinus, Salicaceae, Tiges de plante.
- métabolisme : Acides caféiques, Acides coumariques, Acyl coenzyme A, Coenzyme A ligases, Isoenzymes, Protéines recombinantes.
- Cinétique, Clonage moléculaire, Hybridation in situ, Régions promotrices (génétique), Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux.
English descriptors
- KwdEn :
- Acyl Coenzyme A (metabolism), Caffeic Acids (metabolism), Cloning, Molecular (MeSH), Coenzyme A Ligases (genetics), Coenzyme A Ligases (metabolism), Coumaric Acids (metabolism), Flavonoids (biosynthesis), Flavonoids (chemistry), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), In Situ Hybridization (MeSH), Isoenzymes (genetics), Isoenzymes (metabolism), Kinetics (MeSH), Lignin (biosynthesis), Lignin (chemistry), Pinus (enzymology), Pinus (genetics), Plant Stems (cytology), Plant Stems (enzymology), Plant Stems (genetics), Promoter Regions, Genetic (MeSH), Recombinant Proteins (metabolism), Salicaceae (enzymology), Salicaceae (genetics).
- MESH :
- chemical , biosynthesis : Flavonoids, Lignin.
- chemical , chemistry : Flavonoids, Lignin.
- chemical , genetics : Coenzyme A Ligases, Isoenzymes.
- chemical , metabolism : Acyl Coenzyme A, Caffeic Acids, Coenzyme A Ligases, Coumaric Acids, Isoenzymes, Recombinant Proteins.
- cytology : Plant Stems.
- enzymology : Pinus, Plant Stems, Salicaceae.
- genetics : Pinus, Plant Stems, Salicaceae.
- Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, In Situ Hybridization, Kinetics, Promoter Regions, Genetic.
Abstract
4-Coumarate:coenzyme A ligase (4CL) activates hydroxycinnamates for entry into phenylpropanoid branchways that support various metabolic activities, including lignification and flavonoid biosynthesis. However, it is not clear whether and how 4CL proteins with their broad substrate specificities fulfill the specific hydroxycinnamate requirements of the branchways they supply. Two tissue-specific 4CLs, Pt4CL1 and Pt4CL2, have previously been cloned from quaking aspen (Populus tremuloides Michx.), but whether they are catalytically adapted for the distinctive metabolic roles they are thought to support is not apparent from published biochemical data. Therefore, single- and mixed-substrate assays were conducted to determine whether the 4CLs from aspen exhibit clear catalytic identities under certain metabolic circumstances. Recombinant Pt4CL1 and Pt4CL2 exhibited the expected preference for p-coumarate in single-substrate assays, but strong competitive inhibition favored utilization of caffeate and p-coumarate, respectively, in mixed-substrate assays. The Pt4CL1 product, caffeoyl-CoA, predominated in mixed-substrate assays with xylem extract, and this was consistent with the near absence of Pt4CL2 expression in xylem tissue as determined by in situ hybridization. It is interesting that the Pt4CL2 product p-coumaroyl-CoA predominated in assays with developing leaf extract, although in situ hybridization revealed that both genes were coexpressed. The xylem extract and recombinant 4CL1 data allow us to advance a mechanism by which 4CL1 can selectively utilize caffeate for the support of monolignol biosynthesis in maturing xylem and phloem fibers. Loblolly pine (Pinus taeda), in contrast, possesses a single 4CL protein exhibiting broad substrate specificity in mixed-substrate assays. We discuss these 4CL differences in terms of the contrasts in lignification between angiosperm trees and their gymnosperm progenitors.
DOI: 10.1104/pp.010603
PubMed: 11842147
PubMed Central: PMC148906
Affiliations:
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Le document en format XML
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enzymes</term><term>Régulation de l'expression des gènes végétaux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">4-Coumarate:coenzyme A ligase (4CL) activates hydroxycinnamates for entry into phenylpropanoid branchways that support various metabolic activities, including lignification and flavonoid biosynthesis. However, it is not clear whether and how 4CL proteins with their broad substrate specificities fulfill the specific hydroxycinnamate requirements of the branchways they supply. Two tissue-specific 4CLs, Pt4CL1 and Pt4CL2, have previously been cloned from quaking aspen (Populus tremuloides Michx.), but whether they are catalytically adapted for the distinctive metabolic roles they are thought to support is not apparent from published biochemical data. Therefore, single- and mixed-substrate assays were conducted to determine whether the 4CLs from aspen exhibit clear catalytic identities under certain metabolic circumstances. Recombinant Pt4CL1 and Pt4CL2 exhibited the expected preference for p-coumarate in single-substrate assays, but strong competitive inhibition favored utilization of caffeate and p-coumarate, respectively, in mixed-substrate assays. The Pt4CL1 product, caffeoyl-CoA, predominated in mixed-substrate assays with xylem extract, and this was consistent with the near absence of Pt4CL2 expression in xylem tissue as determined by in situ hybridization. It is interesting that the Pt4CL2 product p-coumaroyl-CoA predominated in assays with developing leaf extract, although in situ hybridization revealed that both genes were coexpressed. The xylem extract and recombinant 4CL1 data allow us to advance a mechanism by which 4CL1 can selectively utilize caffeate for the support of monolignol biosynthesis in maturing xylem and phloem fibers. Loblolly pine (Pinus taeda), in contrast, possesses a single 4CL protein exhibiting broad substrate specificity in mixed-substrate assays. We discuss these 4CL differences in terms of the contrasts in lignification between angiosperm trees and their gymnosperm progenitors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11842147</PMID><DateCompleted><Year>2002</Year><Month>06</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>128</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Differential substrate inhibition couples kinetically distinct 4-coumarate:coenzyme a ligases with spatially distinct metabolic roles in quaking aspen.</ArticleTitle><Pagination><MedlinePgn>428-38</MedlinePgn></Pagination><Abstract><AbstractText>4-Coumarate:coenzyme A ligase (4CL) activates hydroxycinnamates for entry into phenylpropanoid branchways that support various metabolic activities, including lignification and flavonoid biosynthesis. However, it is not clear whether and how 4CL proteins with their broad substrate specificities fulfill the specific hydroxycinnamate requirements of the branchways they supply. Two tissue-specific 4CLs, Pt4CL1 and Pt4CL2, have previously been cloned from quaking aspen (Populus tremuloides Michx.), but whether they are catalytically adapted for the distinctive metabolic roles they are thought to support is not apparent from published biochemical data. Therefore, single- and mixed-substrate assays were conducted to determine whether the 4CLs from aspen exhibit clear catalytic identities under certain metabolic circumstances. Recombinant Pt4CL1 and Pt4CL2 exhibited the expected preference for p-coumarate in single-substrate assays, but strong competitive inhibition favored utilization of caffeate and p-coumarate, respectively, in mixed-substrate assays. The Pt4CL1 product, caffeoyl-CoA, predominated in mixed-substrate assays with xylem extract, and this was consistent with the near absence of Pt4CL2 expression in xylem tissue as determined by in situ hybridization. It is interesting that the Pt4CL2 product p-coumaroyl-CoA predominated in assays with developing leaf extract, although in situ hybridization revealed that both genes were coexpressed. The xylem extract and recombinant 4CL1 data allow us to advance a mechanism by which 4CL1 can selectively utilize caffeate for the support of monolignol biosynthesis in maturing xylem and phloem fibers. Loblolly pine (Pinus taeda), in contrast, possesses a single 4CL protein exhibiting broad substrate specificity in mixed-substrate assays. We discuss these 4CL differences in terms of the contrasts in lignification between angiosperm trees and their gymnosperm progenitors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Harding</LastName><ForeName>Scott A</ForeName><Initials>SA</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>Leshkevich</LastName><ForeName>Jacqueline</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>Vincent L</ForeName><Initials>VL</Initials></Author><Author ValidYN="Y"><LastName>Tsai</LastName><ForeName>Chung-Jui</ForeName><Initials>CJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</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="D000214">Acyl Coenzyme A</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002109">Caffeic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003373">Coumaric Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005419">Flavonoids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C119167">feruloyl-CoA</NameOfSubstance></Chemical><Chemical><RegistryNumber>1782-55-4</RegistryNumber><NameOfSubstance UI="C071744">5-hydroxyferulic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>53034-79-0</RegistryNumber><NameOfSubstance UI="C058645">caffeoyl-coenzyme A</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>AVM951ZWST</RegistryNumber><NameOfSubstance UI="C004999">ferulic acid</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>U2S3A33KVM</RegistryNumber><NameOfSubstance UI="C040048">caffeic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000214" MajorTopicYN="N">Acyl Coenzyme A</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002109" MajorTopicYN="N">Caffeic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003066" MajorTopicYN="N">Coenzyme A Ligases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003373" MajorTopicYN="N">Coumaric Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005419" MajorTopicYN="N">Flavonoids</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017403" MajorTopicYN="N">In Situ Hybridization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D028223" MajorTopicYN="N">Pinus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018547" MajorTopicYN="N">Plant Stems</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011401" MajorTopicYN="N">Promoter Regions, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D031308" MajorTopicYN="N">Salicaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>2</Month><Day>14</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>6</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>2</Month><Day>14</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11842147</ArticleId><ArticleId IdType="doi">10.1104/pp.010603</ArticleId><ArticleId IdType="pmc">PMC148906</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Planta. 1996;200(1):13-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8987616</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1977 Nov;184(1):237-48</Citation><ArticleIdList><ArticleId IdType="pubmed">921295</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1997 Feb;113(2):321-325</Citation><ArticleIdList><ArticleId IdType="pubmed">12223610</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1993 Aug;102(4):1147-56</Citation><ArticleIdList><ArticleId 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Chiang</name><name sortKey="Leshkevich, Jacqueline" sort="Leshkevich, Jacqueline" uniqKey="Leshkevich J" first="Jacqueline" last="Leshkevich">Jacqueline Leshkevich</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="Harding, Scott A" sort="Harding, Scott A" uniqKey="Harding S" first="Scott A" last="Harding">Scott A. Harding</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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