Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures
An elicitor-inducible sesquiterpene cyclase, which catalyzes the conversion of farnesyl diphosphate to 5-epi-aristolochene (IM Whitehead, DR Threlfall, DF Ewing [1989] Phytochemistry 28:775-779) and representing a committed step in the phytoalexin biosynthetic pathway in tobacco, was purified by a c...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1990-05, Vol.93 (1), p.182-187 |
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| creator | Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland) Freeman, J.W Chappell, J |
| description | An elicitor-inducible sesquiterpene cyclase, which catalyzes the conversion of farnesyl diphosphate to 5-epi-aristolochene (IM Whitehead, DR Threlfall, DF Ewing [1989] Phytochemistry 28:775-779) and representing a committed step in the phytoalexin biosynthetic pathway in tobacco, was purified by a combination of hydrophobic interaction, anion exchange, hydroxylapatite, and chromatofocusing chromatography. From 2 kgms of elicited tobacco (Nicotiana tabacum) cells, approximately 500 micrograms of cyclase protein was purified, representing greater than a 130-fold increase in the specific activity of the enzyme and a 4% recovery of the starting activity. The purified enzyme resolved as two major polypeptides of 60 and 62 kilodaltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Biochemical characterization of the enzyme activity included an absolute requirement for magnesium, an isoelectric point of 4.5 to 4.9, and a Km for farnesyl diphosphate of 2 to 5 micromolar. The purified cyclase protein was used to generate mouse polyclonal antibodies which efficiently inhibited cyclase activity in an in vitro assay. Electrophoresis of extracts from elicitor-treated cells or purified cyclase enzyme on native polyacrylamide gels separated the cyclase enzyme into four polypeptides as shown by immunoblot analysis using poly- and monoclonal antibodies. Proportionate cyclase enzyme activity comigrated with those polypeptides. No cyclase polypeptides were detectable in extracts of control cells by immunoblot analysis. However, immunoblot analysis of proteins from elicitor-treated cells using 4 independent monoclonal antibody lines and the polyclonal antibodies detected the same polypeptides, regardless of whether the proteins were separated by native or SDS-PAGE. The results suggest an induction of multiple cyclase polypeptides in elicitor-treated cells resulting from either the expression of multiple genes or multiple post-translational processing events |
| doi_str_mv | 10.1104/pp.93.1.182 |
| format | Article |
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(Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland) ; Freeman, J.W ; Chappell, J</creator><creatorcontrib>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland) ; Freeman, J.W ; Chappell, J</creatorcontrib><description>An elicitor-inducible sesquiterpene cyclase, which catalyzes the conversion of farnesyl diphosphate to 5-epi-aristolochene (IM Whitehead, DR Threlfall, DF Ewing [1989] Phytochemistry 28:775-779) and representing a committed step in the phytoalexin biosynthetic pathway in tobacco, was purified by a combination of hydrophobic interaction, anion exchange, hydroxylapatite, and chromatofocusing chromatography. From 2 kgms of elicited tobacco (Nicotiana tabacum) cells, approximately 500 micrograms of cyclase protein was purified, representing greater than a 130-fold increase in the specific activity of the enzyme and a 4% recovery of the starting activity. The purified enzyme resolved as two major polypeptides of 60 and 62 kilodaltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Biochemical characterization of the enzyme activity included an absolute requirement for magnesium, an isoelectric point of 4.5 to 4.9, and a Km for farnesyl diphosphate of 2 to 5 micromolar. The purified cyclase protein was used to generate mouse polyclonal antibodies which efficiently inhibited cyclase activity in an in vitro assay. Electrophoresis of extracts from elicitor-treated cells or purified cyclase enzyme on native polyacrylamide gels separated the cyclase enzyme into four polypeptides as shown by immunoblot analysis using poly- and monoclonal antibodies. Proportionate cyclase enzyme activity comigrated with those polypeptides. No cyclase polypeptides were detectable in extracts of control cells by immunoblot analysis. However, immunoblot analysis of proteins from elicitor-treated cells using 4 independent monoclonal antibody lines and the polyclonal antibodies detected the same polypeptides, regardless of whether the proteins were separated by native or SDS-PAGE. The results suggest an induction of multiple cyclase polypeptides in elicitor-treated cells resulting from either the expression of multiple genes or multiple post-translational processing events</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.93.1.182</identifier><identifier>PMID: 16667432</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>ACTIVIDAD CATALITICA ; ACTIVIDAD ENZIMATICA ; ACTIVITE CATALYTIQUE ; ACTIVITE ENZYMATIQUE ; Agronomy. Soil science and plant productions ; ANALISIS ; ANALYSE ; Biological and medical sciences ; BIOSINTESIS ; BIOSYNTHESE ; Cell culture techniques ; CELLULASE ; CELULASA ; Chromatography ; CULTIVO DE TEJIDOS ; CULTURE DE TISSUS ; Cultured cells ; Enzyme activity ; Enzymes ; EPURATION ; FITOALEXINA ; Fundamental and applied biological sciences. Psychology ; Gels ; Genetics and breeding of economic plants ; HYDROLYSAT DE PROTEINES ; Microbe-Plant Interactions ; Monoclonal antibodies ; NICOTIANA TABACUM ; Pest resistance ; PHYTOALEXINE ; Plant biochemistry ; Plant pathogens ; Plants ; PROTEINAS ; PROTEINAS HIDROLIZADAS ; PROTEINE ; PURIFICACION ; Sesquiterpenes ; Varietal selection. Specialized plant breeding, plant breeding aims</subject><ispartof>Plant physiology (Bethesda), 1990-05, Vol.93 (1), p.182-187</ispartof><rights>Copyright 1990 American Society of Plant Physiologists</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-1c909886267c16fd93ba9f4dd013fef37538aed6e900c9a0d9447e2c7e78f92b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4272800$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4272800$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27923,27924,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19258144$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16667432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland)</creatorcontrib><creatorcontrib>Freeman, J.W</creatorcontrib><creatorcontrib>Chappell, J</creatorcontrib><title>Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>An elicitor-inducible sesquiterpene cyclase, which catalyzes the conversion of farnesyl diphosphate to 5-epi-aristolochene (IM Whitehead, DR Threlfall, DF Ewing [1989] Phytochemistry 28:775-779) and representing a committed step in the phytoalexin biosynthetic pathway in tobacco, was purified by a combination of hydrophobic interaction, anion exchange, hydroxylapatite, and chromatofocusing chromatography. From 2 kgms of elicited tobacco (Nicotiana tabacum) cells, approximately 500 micrograms of cyclase protein was purified, representing greater than a 130-fold increase in the specific activity of the enzyme and a 4% recovery of the starting activity. The purified enzyme resolved as two major polypeptides of 60 and 62 kilodaltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Biochemical characterization of the enzyme activity included an absolute requirement for magnesium, an isoelectric point of 4.5 to 4.9, and a Km for farnesyl diphosphate of 2 to 5 micromolar. The purified cyclase protein was used to generate mouse polyclonal antibodies which efficiently inhibited cyclase activity in an in vitro assay. Electrophoresis of extracts from elicitor-treated cells or purified cyclase enzyme on native polyacrylamide gels separated the cyclase enzyme into four polypeptides as shown by immunoblot analysis using poly- and monoclonal antibodies. Proportionate cyclase enzyme activity comigrated with those polypeptides. No cyclase polypeptides were detectable in extracts of control cells by immunoblot analysis. However, immunoblot analysis of proteins from elicitor-treated cells using 4 independent monoclonal antibody lines and the polyclonal antibodies detected the same polypeptides, regardless of whether the proteins were separated by native or SDS-PAGE. The results suggest an induction of multiple cyclase polypeptides in elicitor-treated cells resulting from either the expression of multiple genes or multiple post-translational processing events</description><subject>ACTIVIDAD CATALITICA</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE CATALYTIQUE</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Agronomy. Soil science and plant productions</subject><subject>ANALISIS</subject><subject>ANALYSE</subject><subject>Biological and medical sciences</subject><subject>BIOSINTESIS</subject><subject>BIOSYNTHESE</subject><subject>Cell culture techniques</subject><subject>CELLULASE</subject><subject>CELULASA</subject><subject>Chromatography</subject><subject>CULTIVO DE TEJIDOS</subject><subject>CULTURE DE TISSUS</subject><subject>Cultured cells</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>EPURATION</subject><subject>FITOALEXINA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Genetics and breeding of economic plants</subject><subject>HYDROLYSAT DE PROTEINES</subject><subject>Microbe-Plant Interactions</subject><subject>Monoclonal antibodies</subject><subject>NICOTIANA TABACUM</subject><subject>Pest resistance</subject><subject>PHYTOALEXINE</subject><subject>Plant biochemistry</subject><subject>Plant pathogens</subject><subject>Plants</subject><subject>PROTEINAS</subject><subject>PROTEINAS HIDROLIZADAS</subject><subject>PROTEINE</subject><subject>PURIFICACION</subject><subject>Sesquiterpenes</subject><subject>Varietal selection. Specialized plant breeding, plant breeding aims</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNpVks1rFTEUxYMo9vXpyp2IZCMuZJ75mplkI0ipH1BQ0K7DncxNmzJvMk1mhLrwbzePebS6yuWeX05yOZeQF5ztOGfq_TTtjNzxHdfiEdnwWopK1Eo_JhvGSs20NifkNOcbxhiXXD0lJ7xpmlZJsSF_vi8p-OBgDnGkMPbUXUMCN2MKv9dm9KVPw9gvLnQD0oz5dgkFmHBE6u7cABmpT3FPcQguzDFVc0KYsadz7MC5SB0OA81LLlfywdMtw7wkzM_IEw9DxufHc0suP53_PPtSXXz7_PXs40XlamXmijvDjNaNaFrHG98b2YHxqu_LQB69bGupAfsGDWPOAOuNUi0K12KrvRGd3JIPq--0dHvsHY5zgsFOKewh3dkIwf6vjOHaXsVflrNGKN0Ug7dHgxRvF8yz3Yd8mApGjEu2rZTKiIIW8t1KuhRzTujvX-HMHgKz02SNtNyWwAr9-t-PPbDHhArw5ghAdjD4BKML-YEzotZcqcK9WrmbXAK415VohS57sCUvV9lDtHCVisXlD8MUYzWXfwGCJbRI</recordid><startdate>19900501</startdate><enddate>19900501</enddate><creator>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland)</creator><creator>Freeman, J.W</creator><creator>Chappell, J</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19900501</creationdate><title>Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures</title><author>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland) ; Freeman, J.W ; Chappell, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-1c909886267c16fd93ba9f4dd013fef37538aed6e900c9a0d9447e2c7e78f92b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>ACTIVIDAD CATALITICA</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE CATALYTIQUE</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Agronomy. Soil science and plant productions</topic><topic>ANALISIS</topic><topic>ANALYSE</topic><topic>Biological and medical sciences</topic><topic>BIOSINTESIS</topic><topic>BIOSYNTHESE</topic><topic>Cell culture techniques</topic><topic>CELLULASE</topic><topic>CELULASA</topic><topic>Chromatography</topic><topic>CULTIVO DE TEJIDOS</topic><topic>CULTURE DE TISSUS</topic><topic>Cultured cells</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>EPURATION</topic><topic>FITOALEXINA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Genetics and breeding of economic plants</topic><topic>HYDROLYSAT DE PROTEINES</topic><topic>Microbe-Plant Interactions</topic><topic>Monoclonal antibodies</topic><topic>NICOTIANA TABACUM</topic><topic>Pest resistance</topic><topic>PHYTOALEXINE</topic><topic>Plant biochemistry</topic><topic>Plant pathogens</topic><topic>Plants</topic><topic>PROTEINAS</topic><topic>PROTEINAS HIDROLIZADAS</topic><topic>PROTEINE</topic><topic>PURIFICACION</topic><topic>Sesquiterpenes</topic><topic>Varietal selection. Specialized plant breeding, plant breeding aims</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland)</creatorcontrib><creatorcontrib>Freeman, J.W</creatorcontrib><creatorcontrib>Chappell, J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vogeli, U. (Dr. R. Maag Ltd., Agrochemicals, Dielsdorf, Switzerland)</au><au>Freeman, J.W</au><au>Chappell, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1990-05-01</date><risdate>1990</risdate><volume>93</volume><issue>1</issue><spage>182</spage><epage>187</epage><pages>182-187</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>An elicitor-inducible sesquiterpene cyclase, which catalyzes the conversion of farnesyl diphosphate to 5-epi-aristolochene (IM Whitehead, DR Threlfall, DF Ewing [1989] Phytochemistry 28:775-779) and representing a committed step in the phytoalexin biosynthetic pathway in tobacco, was purified by a combination of hydrophobic interaction, anion exchange, hydroxylapatite, and chromatofocusing chromatography. From 2 kgms of elicited tobacco (Nicotiana tabacum) cells, approximately 500 micrograms of cyclase protein was purified, representing greater than a 130-fold increase in the specific activity of the enzyme and a 4% recovery of the starting activity. The purified enzyme resolved as two major polypeptides of 60 and 62 kilodaltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Biochemical characterization of the enzyme activity included an absolute requirement for magnesium, an isoelectric point of 4.5 to 4.9, and a Km for farnesyl diphosphate of 2 to 5 micromolar. The purified cyclase protein was used to generate mouse polyclonal antibodies which efficiently inhibited cyclase activity in an in vitro assay. Electrophoresis of extracts from elicitor-treated cells or purified cyclase enzyme on native polyacrylamide gels separated the cyclase enzyme into four polypeptides as shown by immunoblot analysis using poly- and monoclonal antibodies. Proportionate cyclase enzyme activity comigrated with those polypeptides. No cyclase polypeptides were detectable in extracts of control cells by immunoblot analysis. However, immunoblot analysis of proteins from elicitor-treated cells using 4 independent monoclonal antibody lines and the polyclonal antibodies detected the same polypeptides, regardless of whether the proteins were separated by native or SDS-PAGE. The results suggest an induction of multiple cyclase polypeptides in elicitor-treated cells resulting from either the expression of multiple genes or multiple post-translational processing events</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16667432</pmid><doi>10.1104/pp.93.1.182</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 1990-05, Vol.93 (1), p.182-187 |
| issn | 0032-0889 1532-2548 |
| language | eng |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; JSTOR Archive Collection A-Z Listing; Alma/SFX Local Collection |
| subjects | ACTIVIDAD CATALITICA ACTIVIDAD ENZIMATICA ACTIVITE CATALYTIQUE ACTIVITE ENZYMATIQUE Agronomy. Soil science and plant productions ANALISIS ANALYSE Biological and medical sciences BIOSINTESIS BIOSYNTHESE Cell culture techniques CELLULASE CELULASA Chromatography CULTIVO DE TEJIDOS CULTURE DE TISSUS Cultured cells Enzyme activity Enzymes EPURATION FITOALEXINA Fundamental and applied biological sciences. Psychology Gels Genetics and breeding of economic plants HYDROLYSAT DE PROTEINES Microbe-Plant Interactions Monoclonal antibodies NICOTIANA TABACUM Pest resistance PHYTOALEXINE Plant biochemistry Plant pathogens Plants PROTEINAS PROTEINAS HIDROLIZADAS PROTEINE PURIFICACION Sesquiterpenes Varietal selection. Specialized plant breeding, plant breeding aims |
| title | Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures |
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