Biochemical properties of isoprene synthase in poplar (Populus x canescens).
Identifieur interne : 004099 ( Main/Exploration ); précédent : 004098; suivant : 004100Biochemical properties of isoprene synthase in poplar (Populus x canescens).
Auteurs : J-P Schnitzler [Allemagne] ; I. Zimmer ; A. Bachl ; M. Arend ; J. Fromm ; R J FischbachSource :
- Planta [ 0032-0935 ] ; 2005.
Descripteurs français
- KwdFr :
- Alkyl et aryl transferases (composition chimique), Alkyl et aryl transferases (génétique), Alkyl et aryl transferases (isolement et purification), Alkyl et aryl transferases (métabolisme), Cinétique (MeSH), Distribution tissulaire (MeSH), Immunochimie (MeSH), Populus (enzymologie), Populus (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Spécificité du substrat (MeSH).
- MESH :
- composition chimique : Alkyl et aryl transferases, Protéines recombinantes.
- enzymologie : Populus.
- génétique : Alkyl et aryl transferases, Populus, Protéines recombinantes.
- isolement et purification : Alkyl et aryl transferases.
- métabolisme : Alkyl et aryl transferases.
- Cinétique, Distribution tissulaire, Immunochimie, Spécificité du substrat.
English descriptors
- KwdEn :
- Alkyl and Aryl Transferases (chemistry), Alkyl and Aryl Transferases (genetics), Alkyl and Aryl Transferases (isolation & purification), Alkyl and Aryl Transferases (metabolism), Immunochemistry (MeSH), Kinetics (MeSH), Populus (enzymology), Populus (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Substrate Specificity (MeSH), Tissue Distribution (MeSH).
- MESH :
- chemical , chemistry : Alkyl and Aryl Transferases, Recombinant Proteins.
- chemical , genetics : Alkyl and Aryl Transferases, Recombinant Proteins.
- chemical , isolation & purification : Alkyl and Aryl Transferases.
- chemical , metabolism : Alkyl and Aryl Transferases.
- enzymology : Populus.
- genetics : Populus.
- Immunochemistry, Kinetics, Substrate Specificity, Tissue Distribution.
Abstract
Isoprene synthase (ISPS) catalyzes the elimination of pyrophosphate from dimethylallyl diphosphate (DMADP) forming isoprene, a volatile hydrocarbon emitted from many plant species to the atmosphere. In the present work, immunological techniques were applied to study and localize ISPS in poplar leaves (Populus x canescens). Immunogold labeling using polyclonal antibodies generated against His-tagged recombinant ISPS protein detected ca. 44% of ISPS in the stroma of the chloroplasts and ca. 56% of gold particles attached to the stromal-facing side of the thylakoid membranes. ISPS isolated from leaves exhibited the same biochemical properties as the recombinant ISPS without the plastid-targeting peptide heterologous expressed in E. coli, whereas an additional C- or N-terminal His-tag changed the biochemical features of the recombinant enzyme with regard to temperature, pH, and substrate dependence. In comparison to the closely related class of monoterpene synthases from angiosperms and ISPS of oaks, the most striking feature of the poplar ISPS is a cooperative substrate dependence which is characteristic to enzymes with positive substrate activation. The detection of four immunoreactive bands in poplar leaf extracts with isoelectric points from 5.0 to 5.5 and a native molecular weight of ca. 51 kDa give reason for future studies on post-translational modifications of ISPS.
DOI: 10.1007/s00425-005-0022-1
PubMed: 16052321
Affiliations:
Links toward previous steps (curation, corpus...)
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Zimmer</name></author><author><name sortKey="Bachl, A" sort="Bachl, A" uniqKey="Bachl A" first="A" last="Bachl">A. Bachl</name></author><author><name sortKey="Arend, M" sort="Arend, M" uniqKey="Arend M" first="M" last="Arend">M. Arend</name></author><author><name sortKey="Fromm, J" sort="Fromm, J" uniqKey="Fromm J" first="J" last="Fromm">J. Fromm</name></author><author><name sortKey="Fischbach, R J" sort="Fischbach, R J" uniqKey="Fischbach R" first="R J" last="Fischbach">R J Fischbach</name></author></analytic><series><title level="j">Planta</title><idno type="ISSN">0032-0935</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alkyl and Aryl Transferases (chemistry)</term><term>Alkyl and Aryl Transferases (genetics)</term><term>Alkyl and Aryl Transferases (isolation & purification)</term><term>Alkyl and Aryl Transferases (metabolism)</term><term>Immunochemistry (MeSH)</term><term>Kinetics (MeSH)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Substrate Specificity (MeSH)</term><term>Tissue Distribution (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alkyl et aryl transferases (composition chimique)</term><term>Alkyl et aryl transferases (génétique)</term><term>Alkyl et aryl transferases (isolement et purification)</term><term>Alkyl et aryl transferases (métabolisme)</term><term>Cinétique (MeSH)</term><term>Distribution tissulaire (MeSH)</term><term>Immunochimie (MeSH)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alkyl and Aryl Transferases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alkyl and Aryl Transferases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Alkyl and Aryl Transferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alkyl and Aryl Transferases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Alkyl et aryl transferases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alkyl et aryl transferases</term><term>Populus</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Alkyl et aryl transferases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alkyl et aryl transferases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Immunochemistry</term><term>Kinetics</term><term>Substrate Specificity</term><term>Tissue Distribution</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Distribution tissulaire</term><term>Immunochimie</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Isoprene synthase (ISPS) catalyzes the elimination of pyrophosphate from dimethylallyl diphosphate (DMADP) forming isoprene, a volatile hydrocarbon emitted from many plant species to the atmosphere. In the present work, immunological techniques were applied to study and localize ISPS in poplar leaves (Populus x canescens). Immunogold labeling using polyclonal antibodies generated against His-tagged recombinant ISPS protein detected ca. 44% of ISPS in the stroma of the chloroplasts and ca. 56% of gold particles attached to the stromal-facing side of the thylakoid membranes. ISPS isolated from leaves exhibited the same biochemical properties as the recombinant ISPS without the plastid-targeting peptide heterologous expressed in E. coli, whereas an additional C- or N-terminal His-tag changed the biochemical features of the recombinant enzyme with regard to temperature, pH, and substrate dependence. In comparison to the closely related class of monoterpene synthases from angiosperms and ISPS of oaks, the most striking feature of the poplar ISPS is a cooperative substrate dependence which is characteristic to enzymes with positive substrate activation. The detection of four immunoreactive bands in poplar leaf extracts with isoelectric points from 5.0 to 5.5 and a native molecular weight of ca. 51 kDa give reason for future studies on post-translational modifications of ISPS.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16052321</PMID><DateCompleted><Year>2006</Year><Month>01</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0032-0935</ISSN><JournalIssue CitedMedium="Print"><Volume>222</Volume><Issue>5</Issue><PubDate><Year>2005</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Biochemical properties of isoprene synthase in poplar (Populus x canescens).</ArticleTitle><Pagination><MedlinePgn>777-86</MedlinePgn></Pagination><Abstract><AbstractText>Isoprene synthase (ISPS) catalyzes the elimination of pyrophosphate from dimethylallyl diphosphate (DMADP) forming isoprene, a volatile hydrocarbon emitted from many plant species to the atmosphere. In the present work, immunological techniques were applied to study and localize ISPS in poplar leaves (Populus x canescens). Immunogold labeling using polyclonal antibodies generated against His-tagged recombinant ISPS protein detected ca. 44% of ISPS in the stroma of the chloroplasts and ca. 56% of gold particles attached to the stromal-facing side of the thylakoid membranes. ISPS isolated from leaves exhibited the same biochemical properties as the recombinant ISPS without the plastid-targeting peptide heterologous expressed in E. coli, whereas an additional C- or N-terminal His-tag changed the biochemical features of the recombinant enzyme with regard to temperature, pH, and substrate dependence. In comparison to the closely related class of monoterpene synthases from angiosperms and ISPS of oaks, the most striking feature of the poplar ISPS is a cooperative substrate dependence which is characteristic to enzymes with positive substrate activation. The detection of four immunoreactive bands in poplar leaf extracts with isoelectric points from 5.0 to 5.5 and a native molecular weight of ca. 51 kDa give reason for future studies on post-translational modifications of ISPS.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schnitzler</LastName><ForeName>J-P</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Forschungszentrum Karlsruhe GmbH, Institut für Meteorologie und Klimaforschung, Atmosphärische Umweltforschung (IMK-IFU), Kreuzeckbahnstr. 19, 82467, Garmisch-Partenkirchen, Germany. joerg-peter.schnitzler@imk.fzk.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zimmer</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Bachl</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Arend</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fromm</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Fischbach</LastName><ForeName>R J</ForeName><Initials>RJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>07</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.-</RegistryNumber><NameOfSubstance UI="D019883">Alkyl and Aryl Transferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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Arend</name><name sortKey="Bachl, A" sort="Bachl, A" uniqKey="Bachl A" first="A" last="Bachl">A. Bachl</name><name sortKey="Fischbach, R J" sort="Fischbach, R J" uniqKey="Fischbach R" first="R J" last="Fischbach">R J Fischbach</name><name sortKey="Fromm, J" sort="Fromm, J" uniqKey="Fromm J" first="J" last="Fromm">J. Fromm</name><name sortKey="Zimmer, I" sort="Zimmer, I" uniqKey="Zimmer I" first="I" last="Zimmer">I. Zimmer</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Schnitzler, J P" sort="Schnitzler, J P" uniqKey="Schnitzler J" first="J-P" last="Schnitzler">J-P Schnitzler</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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