Molecular cloning and heterologous expression of acridone synthase from elicited Ruta graveolens L. cell suspension cultures.
Identifieur interne : 002B73 ( Main/Exploration ); précédent : 002B72; suivant : 002B74Molecular cloning and heterologous expression of acridone synthase from elicited Ruta graveolens L. cell suspension cultures.
Auteurs : K T Junghanns [Allemagne] ; R E Kneusel ; A. Baumert ; W. Maier ; D. Gröger ; U. MaternSource :
- Plant molecular biology [ 0167-4412 ] ; 1995.
Descripteurs français
- KwdFr :
- ADN complémentaire (MeSH), Acyltransferases (génétique), Alignement de séquences (MeSH), Cellules cultivées (MeSH), Cellules végétales (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Plantes (enzymologie), Plantes (génétique), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- enzymologie : Plantes.
- génétique : Acyltransferases, Plantes.
- ADN complémentaire, Alignement de séquences, Cellules cultivées, Cellules végétales, Clonage moléculaire, Données de séquences moléculaires, Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Acyltransferases (genetics), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cells, Cultured (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (MeSH), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Molecular Sequence Data (MeSH), Plant Cells (MeSH), Plants (enzymology), Plants (genetics), Sequence Alignment (MeSH).
- MESH :
- chemical , genetics : Acyltransferases.
- enzymology : Plants.
- genetics : Plants.
- Amino Acid Sequence, Base Sequence, Cells, Cultured, Cloning, Molecular, DNA, Complementary, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Molecular Sequence Data, Plant Cells, Sequence Alignment.
Abstract
Cell suspension cultures of Ruta graveolens L. produce a variety of acridone alkaloids, and the accumulation can be stimulated by the addition of fungal elicitors. Acridone synthase, the enzyme catalyzing the synthesis of 1,3-dihydroxy-N-methylacridone from N-methylanthraniloyl-CoA and malonyl-CoA, had been isolated from these cells, and the partial enzyme polypeptide sequence, elucidated from six tryptic fragments, revealed homology to heterologous chalcone synthases. Poly(A)+ RNA was isolated from Ruta cells that had been treated for 6 h with a crude cell wall elicitor from Phytophthora megasperma f. sp. glycinea, and a cDNA library was constructed in lambda 2AP. Clones harboring acridone synthase cDNA were isolated from the library by screening with a synthetic oligonucleotide probe complementary to a short stretch of sequence of the enzyme peptide with negligible homology to chalcone synthases. The identity of the clones was substantiated by DNA sequencing and by recognition of five additional peptides, determined previously from tryptic acridone synthase digests, in the translated sequence. An insert of roughly 1.4 kb encoded the complete acridone synthase, and alignments at both DNA and protein levels corroborated the high degree of homology to chalcone synthases. Expression of the enzyme in vector pET-11c in the Escherichia coli pLysS host strain proved the identity of the cloned cDNA. The heterologous enzyme in the crude E. coli extract exhibit high acridone but no chalcone synthase activity. The results were fully supported by northern blot hybridizations which revealed that the specific transcript abundance did not increase but rather decreased upon white light irradiation of cultured Ruta graveolens L. cells, a condition that commonly induces the abundance of chalcone synthase transcripts.
DOI: 10.1007/BF00020222
PubMed: 7727746
Affiliations:
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Matern</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7727746</idno><idno type="pmid">7727746</idno><idno type="doi">10.1007/BF00020222</idno><idno type="wicri:Area/Main/Corpus">002B91</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002B91</idno><idno type="wicri:Area/Main/Curation">002B91</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002B91</idno><idno type="wicri:Area/Main/Exploration">002B91</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular cloning and heterologous expression of acridone synthase from elicited Ruta graveolens L. cell suspension cultures.</title><author><name sortKey="Junghanns, K T" sort="Junghanns, K T" uniqKey="Junghanns K" first="K T" last="Junghanns">K T Junghanns</name><affiliation wicri:level="3"><nlm:affiliation>Biologisches Institut II, Albert-Ludwigs-Universität, Freiburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Biologisches Institut II, Albert-Ludwigs-Universität, Freiburg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Fribourg-en-Brisgau</region><settlement type="city">Fribourg-en-Brisgau</settlement></placeName></affiliation></author><author><name sortKey="Kneusel, R E" sort="Kneusel, R E" uniqKey="Kneusel R" first="R E" last="Kneusel">R E Kneusel</name></author><author><name sortKey="Baumert, A" sort="Baumert, A" uniqKey="Baumert A" first="A" last="Baumert">A. Baumert</name></author><author><name sortKey="Maier, W" sort="Maier, W" uniqKey="Maier W" first="W" last="Maier">W. Maier</name></author><author><name sortKey="Groger, D" sort="Groger, D" uniqKey="Groger D" first="D" last="Gröger">D. Gröger</name></author><author><name sortKey="Matern, U" sort="Matern, U" uniqKey="Matern U" first="U" last="Matern">U. Matern</name></author></analytic><series><title level="j">Plant molecular biology</title><idno type="ISSN">0167-4412</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acyltransferases (genetics)</term><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (MeSH)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Cells (MeSH)</term><term>Plants (enzymology)</term><term>Plants (genetics)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (MeSH)</term><term>Acyltransferases (génétique)</term><term>Alignement de séquences (MeSH)</term><term>Cellules cultivées (MeSH)</term><term>Cellules végétales (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Plantes (enzymologie)</term><term>Plantes (génétique)</term><term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acyltransferases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acyltransferases</term><term>Plantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cells, Cultured</term><term>Cloning, Molecular</term><term>DNA, Complementary</term><term>Gene Expression Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term><term>Molecular Sequence Data</term><term>Plant Cells</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN complémentaire</term><term>Alignement de séquences</term><term>Cellules cultivées</term><term>Cellules végétales</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation de l'expression des gènes végétaux</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cell suspension cultures of Ruta graveolens L. produce a variety of acridone alkaloids, and the accumulation can be stimulated by the addition of fungal elicitors. Acridone synthase, the enzyme catalyzing the synthesis of 1,3-dihydroxy-N-methylacridone from N-methylanthraniloyl-CoA and malonyl-CoA, had been isolated from these cells, and the partial enzyme polypeptide sequence, elucidated from six tryptic fragments, revealed homology to heterologous chalcone synthases. Poly(A)+ RNA was isolated from Ruta cells that had been treated for 6 h with a crude cell wall elicitor from Phytophthora megasperma f. sp. glycinea, and a cDNA library was constructed in lambda 2AP. Clones harboring acridone synthase cDNA were isolated from the library by screening with a synthetic oligonucleotide probe complementary to a short stretch of sequence of the enzyme peptide with negligible homology to chalcone synthases. The identity of the clones was substantiated by DNA sequencing and by recognition of five additional peptides, determined previously from tryptic acridone synthase digests, in the translated sequence. An insert of roughly 1.4 kb encoded the complete acridone synthase, and alignments at both DNA and protein levels corroborated the high degree of homology to chalcone synthases. Expression of the enzyme in vector pET-11c in the Escherichia coli pLysS host strain proved the identity of the cloned cDNA. The heterologous enzyme in the crude E. coli extract exhibit high acridone but no chalcone synthase activity. The results were fully supported by northern blot hybridizations which revealed that the specific transcript abundance did not increase but rather decreased upon white light irradiation of cultured Ruta graveolens L. cells, a condition that commonly induces the abundance of chalcone synthase transcripts.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7727746</PMID><DateCompleted><Year>1995</Year><Month>05</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0167-4412</ISSN><JournalIssue CitedMedium="Print"><Volume>27</Volume><Issue>4</Issue><PubDate><Year>1995</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant molecular biology</Title><ISOAbbreviation>Plant Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Molecular cloning and heterologous expression of acridone synthase from elicited Ruta graveolens L. cell suspension cultures.</ArticleTitle><Pagination><MedlinePgn>681-92</MedlinePgn></Pagination><Abstract><AbstractText>Cell suspension cultures of Ruta graveolens L. produce a variety of acridone alkaloids, and the accumulation can be stimulated by the addition of fungal elicitors. Acridone synthase, the enzyme catalyzing the synthesis of 1,3-dihydroxy-N-methylacridone from N-methylanthraniloyl-CoA and malonyl-CoA, had been isolated from these cells, and the partial enzyme polypeptide sequence, elucidated from six tryptic fragments, revealed homology to heterologous chalcone synthases. Poly(A)+ RNA was isolated from Ruta cells that had been treated for 6 h with a crude cell wall elicitor from Phytophthora megasperma f. sp. glycinea, and a cDNA library was constructed in lambda 2AP. Clones harboring acridone synthase cDNA were isolated from the library by screening with a synthetic oligonucleotide probe complementary to a short stretch of sequence of the enzyme peptide with negligible homology to chalcone synthases. The identity of the clones was substantiated by DNA sequencing and by recognition of five additional peptides, determined previously from tryptic acridone synthase digests, in the translated sequence. An insert of roughly 1.4 kb encoded the complete acridone synthase, and alignments at both DNA and protein levels corroborated the high degree of homology to chalcone synthases. Expression of the enzyme in vector pET-11c in the Escherichia coli pLysS host strain proved the identity of the cloned cDNA. The heterologous enzyme in the crude E. coli extract exhibit high acridone but no chalcone synthase activity. The results were fully supported by northern blot hybridizations which revealed that the specific transcript abundance did not increase but rather decreased upon white light irradiation of cultured Ruta graveolens L. cells, a condition that commonly induces the abundance of chalcone synthase transcripts.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Junghanns</LastName><ForeName>K T</ForeName><Initials>KT</Initials><AffiliationInfo><Affiliation>Biologisches Institut II, Albert-Ludwigs-Universität, Freiburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kneusel</LastName><ForeName>R E</ForeName><Initials>RE</Initials></Author><Author ValidYN="Y"><LastName>Baumert</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Maier</LastName><ForeName>W</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Gröger</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Matern</LastName><ForeName>U</ForeName><Initials>U</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>Z34088</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Plant Mol Biol</MedlineTA><NlmUniqueID>9106343</NlmUniqueID><ISSNLinking>0167-4412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.-</RegistryNumber><NameOfSubstance 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Baumert</name><name sortKey="Groger, D" sort="Groger, D" uniqKey="Groger D" first="D" last="Gröger">D. Gröger</name><name sortKey="Kneusel, R E" sort="Kneusel, R E" uniqKey="Kneusel R" first="R E" last="Kneusel">R E Kneusel</name><name sortKey="Maier, W" sort="Maier, W" uniqKey="Maier W" first="W" last="Maier">W. Maier</name><name sortKey="Matern, U" sort="Matern, U" uniqKey="Matern U" first="U" last="Matern">U. Matern</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Junghanns, K T" sort="Junghanns, K T" uniqKey="Junghanns K" first="K T" last="Junghanns">K T Junghanns</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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