Rapid Activation of Phenylpropanoid Metabolism in Elicitor-Treated Hybrid Poplar (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) Suspension-Cultured Cells.
Identifieur interne : 004C03 ( Main/Exploration ); précédent : 004C02; suivant : 004C04Rapid Activation of Phenylpropanoid Metabolism in Elicitor-Treated Hybrid Poplar (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) Suspension-Cultured Cells.
Auteurs : M M De Sá [Canada] ; R. Subramaniam ; F E Williams ; C J DouglasSource :
- Plant physiology [ 0032-0889 ] ; 1992.
Abstract
Elicitor induction of phenylpropanoid metabolism was investigated in suspension-cultured cells of the fast-growing poplar hybrid (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) H11-11. Treatment of cells with polygalacturonic acid lyase or two fungal elicitors resulted in rapid and transient increases in extractable l-phenylalanine ammonia lyase and 4-coumarate:coenzyme A ligase enzyme activities. The substrate specificity of the inducible 4-coumarate:coenzyme A ligase enzyme activity appeared to differ from substrate specificity of 4-coumarate:coenzyme A ligase enzyme activity in untreated control cells. Large and transient increases in the accumulation of l-phenylalanine ammonia-lyase and 4-coumarate:coenzyme A ligase mRNAs preceded the increases in enzyme activities and were detectable by 30 minutes after the start of elicitor treatment. Chalcone synthase, cinnamyl alcohol dehydrogenase, and coniferin beta-glucosidase enzyme activities were unaffected by the elicitors, but a large and transient increase in beta-glucosidase activity capable of hydrolyzing 4-nitrophenyl-beta-glucoside was observed. Subsequent to increases in l-phenylalanine ammonialyase and 4-coumarate:coenzyme A ligase enzyme activities, cell wall-bound thioglycolic acid-extractable compounds accumulated in elicitor-treated cultures, and these cells exhibited strong staining with phloroglucinol, suggesting the accumulation of wall-bound phenolic compounds.
DOI: 10.1104/pp.98.2.728
PubMed: 16668702
PubMed Central: PMC1080251
Affiliations:
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Subramaniam</name></author><author><name sortKey="Williams, F E" sort="Williams, F E" uniqKey="Williams F" first="F E" last="Williams">F E Williams</name></author><author><name sortKey="Douglas, C J" sort="Douglas, C J" uniqKey="Douglas C" first="C J" last="Douglas">C J Douglas</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Elicitor induction of phenylpropanoid metabolism was investigated in suspension-cultured cells of the fast-growing poplar hybrid (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) H11-11. Treatment of cells with polygalacturonic acid lyase or two fungal elicitors resulted in rapid and transient increases in extractable l-phenylalanine ammonia lyase and 4-coumarate:coenzyme A ligase enzyme activities. The substrate specificity of the inducible 4-coumarate:coenzyme A ligase enzyme activity appeared to differ from substrate specificity of 4-coumarate:coenzyme A ligase enzyme activity in untreated control cells. Large and transient increases in the accumulation of l-phenylalanine ammonia-lyase and 4-coumarate:coenzyme A ligase mRNAs preceded the increases in enzyme activities and were detectable by 30 minutes after the start of elicitor treatment. Chalcone synthase, cinnamyl alcohol dehydrogenase, and coniferin beta-glucosidase enzyme activities were unaffected by the elicitors, but a large and transient increase in beta-glucosidase activity capable of hydrolyzing 4-nitrophenyl-beta-glucoside was observed. Subsequent to increases in l-phenylalanine ammonialyase and 4-coumarate:coenzyme A ligase enzyme activities, cell wall-bound thioglycolic acid-extractable compounds accumulated in elicitor-treated cultures, and these cells exhibited strong staining with phloroglucinol, suggesting the accumulation of wall-bound phenolic compounds.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16668702</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>29</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>98</Volume><Issue>2</Issue><PubDate><Year>1992</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Rapid Activation of Phenylpropanoid Metabolism in Elicitor-Treated Hybrid Poplar (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) Suspension-Cultured Cells.</ArticleTitle><Pagination><MedlinePgn>728-37</MedlinePgn></Pagination><Abstract><AbstractText>Elicitor induction of phenylpropanoid metabolism was investigated in suspension-cultured cells of the fast-growing poplar hybrid (Populus trichocarpa Torr. & Gray x Populus deltoides Marsh) H11-11. Treatment of cells with polygalacturonic acid lyase or two fungal elicitors resulted in rapid and transient increases in extractable l-phenylalanine ammonia lyase and 4-coumarate:coenzyme A ligase enzyme activities. The substrate specificity of the inducible 4-coumarate:coenzyme A ligase enzyme activity appeared to differ from substrate specificity of 4-coumarate:coenzyme A ligase enzyme activity in untreated control cells. Large and transient increases in the accumulation of l-phenylalanine ammonia-lyase and 4-coumarate:coenzyme A ligase mRNAs preceded the increases in enzyme activities and were detectable by 30 minutes after the start of elicitor treatment. Chalcone synthase, cinnamyl alcohol dehydrogenase, and coniferin beta-glucosidase enzyme activities were unaffected by the elicitors, but a large and transient increase in beta-glucosidase activity capable of hydrolyzing 4-nitrophenyl-beta-glucoside was observed. Subsequent to increases in l-phenylalanine ammonialyase and 4-coumarate:coenzyme A ligase enzyme activities, cell wall-bound thioglycolic acid-extractable compounds accumulated in elicitor-treated cultures, and these cells exhibited strong staining with phloroglucinol, suggesting the accumulation of wall-bound phenolic compounds.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>de Sá</LastName><ForeName>M M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>University of British Columbia, Department of Botany, Vancouver, British Columbia V6T 1Z4 Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Subramaniam</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>F E</ForeName><Initials>FE</Initials></Author><Author ValidYN="Y"><LastName>Douglas</LastName><ForeName>C J</ForeName><Initials>CJ</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></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16668702</ArticleId><ArticleId IdType="pmc">PMC1080251</ArticleId><ArticleId IdType="doi">10.1104/pp.98.2.728</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Z Naturforsch C. 1975 May-Jun;30(3):352-8</Citation><ArticleIdList><ArticleId IdType="pubmed">126581</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1979 Jan 10;254(1):57-65</Citation><ArticleIdList><ArticleId IdType="pubmed">758324</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1989 Jan 27;56(2):215-24</Citation><ArticleIdList><ArticleId IdType="pubmed">2643475</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1989 Jun;8(6):1641-8</Citation><ArticleIdList><ArticleId IdType="pubmed">2767049</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1989 Oct;86(20):7895-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2813366</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1987 Nov 16;169(1):73-7</Citation><ArticleIdList><ArticleId IdType="pubmed">3315665</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1981 Oct 10;256(19):10061-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7275967</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Plant Physiol Plant Mol Biol. 1990;41:455-96</Citation><ArticleIdList><ArticleId IdType="pubmed">11543592</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1987 May;6(5):1189-95</Citation><ArticleIdList><ArticleId IdType="pubmed">16453765</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1984 Jan;74(1):52-60</Citation><ArticleIdList><ArticleId IdType="pubmed">16663385</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1986 May;81(1):216-21</Citation><ArticleIdList><ArticleId IdType="pubmed">16664778</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1987 Aug;84(4):1286-90</Citation><ArticleIdList><ArticleId IdType="pubmed">16665599</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1987 Sep;85(1):34-41</Citation><ArticleIdList><ArticleId IdType="pubmed">16665678</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1989 Nov;91(3):889-97</Citation><ArticleIdList><ArticleId IdType="pubmed">16667153</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1990 Feb;92(2):440-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16667295</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Colombie-Britannique </li></region><settlement><li>Vancouver</li></settlement><orgName><li>Université de la Colombie-Britannique</li></orgName></list><tree><noCountry><name sortKey="Douglas, C J" sort="Douglas, C J" uniqKey="Douglas C" first="C J" last="Douglas">C J Douglas</name><name sortKey="Subramaniam, R" sort="Subramaniam, R" uniqKey="Subramaniam R" first="R" last="Subramaniam">R. Subramaniam</name><name sortKey="Williams, F E" sort="Williams, F E" uniqKey="Williams F" first="F E" last="Williams">F E Williams</name></noCountry><country name="Canada"><region name="Colombie-Britannique "><name sortKey="De Sa, M M" sort="De Sa, M M" uniqKey="De Sa M" first="M M" last="De Sá">M M De Sá</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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