Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis
cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their...
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| Veröffentlicht in: | Chemical & pharmaceutical bulletin 2001, Vol.49(2), pp.197-202 |
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| creator | SITTHITHAWORN, Worapan KOJIMA, Naoe VIROONCHATAPAN, Ekapop SUH, Dae-Yeon IWANAMI, Naoko HAYASHI, Toshimitsu NOJI, Masaaki SAITO, Kazuki NIWA, Yasuo SANKAWA, Ushio |
| description | cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their N-terminal residues exhibited the characteristics of chloroplast targeting sequence. When expressed in Escherichia coli, both the full-length and truncated proteins in which the putative targeting sequence was deleted catalyzed the condensation of farnesyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate (GGPP). The structural factors determining the product length in plant GGPPSs were investigated by constructing S. dulcis GGPPS mutants on the basis of sequence comparison with the first aspartate-rich motif (FARM) of plant farnesyl diphosphate synthase. The result indicated that in plant GGPPSs small amino acids, Met and Ser, at the fourth and fifth positions before FARM and Pro and Cys insertion in FARM play essential roles in determination of product length. Further, when a chimeric gene comprised of the putative transit peptide of the S. dulcis GGPPS gene and a green fluorescent protein was introduced into Arabidopsis leaves by particle gun bombardment, the chimeric protein was localized in chloroplasts, indicating that the cloned S. dulcis GGPPS is a chloroplast protein. |
| doi_str_mv | 10.1248/cpb.49.197 |
| format | Article |
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Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis</title><source>J-STAGE Free</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>SITTHITHAWORN, Worapan ; KOJIMA, Naoe ; VIROONCHATAPAN, Ekapop ; SUH, Dae-Yeon ; IWANAMI, Naoko ; HAYASHI, Toshimitsu ; NOJI, Masaaki ; SAITO, Kazuki ; NIWA, Yasuo ; SANKAWA, Ushio</creator><creatorcontrib>SITTHITHAWORN, Worapan ; KOJIMA, Naoe ; VIROONCHATAPAN, Ekapop ; SUH, Dae-Yeon ; IWANAMI, Naoko ; HAYASHI, Toshimitsu ; NOJI, Masaaki ; SAITO, Kazuki ; NIWA, Yasuo ; SANKAWA, Ushio</creatorcontrib><description>cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their N-terminal residues exhibited the characteristics of chloroplast targeting sequence. When expressed in Escherichia coli, both the full-length and truncated proteins in which the putative targeting sequence was deleted catalyzed the condensation of farnesyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate (GGPP). The structural factors determining the product length in plant GGPPSs were investigated by constructing S. dulcis GGPPS mutants on the basis of sequence comparison with the first aspartate-rich motif (FARM) of plant farnesyl diphosphate synthase. The result indicated that in plant GGPPSs small amino acids, Met and Ser, at the fourth and fifth positions before FARM and Pro and Cys insertion in FARM play essential roles in determination of product length. Further, when a chimeric gene comprised of the putative transit peptide of the S. dulcis GGPPS gene and a green fluorescent protein was introduced into Arabidopsis leaves by particle gun bombardment, the chimeric protein was localized in chloroplasts, indicating that the cloned S. dulcis GGPPS is a chloroplast protein.</description><identifier>ISSN: 0009-2363</identifier><identifier>EISSN: 1347-5223</identifier><identifier>DOI: 10.1248/cpb.49.197</identifier><identifier>PMID: 11217109</identifier><identifier>CODEN: CPBTAL</identifier><language>eng</language><publisher>Tokyo: The Pharmaceutical Society of Japan</publisher><subject>Alkyl and Aryl Transferases - chemistry ; Alkyl and Aryl Transferases - genetics ; Alkyl and Aryl Transferases - isolation & purification ; Alkyl and Aryl Transferases - metabolism ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; cDNA cloning ; chloroplast localization ; Cloning, Molecular ; DNA Primers ; DNA, Complementary ; Enzymes and enzyme inhibitors ; farnesyl diphosphate synthase ; Farnesyltranstransferase ; Fundamental and applied biological sciences. Psychology ; geranylgeranyl diphosphate synthase ; Geranyltranstransferase ; Magnoliopsida - enzymology ; Magnoliopsida - ultrastructure ; Molecular Sequence Data ; Mutagenesis ; Plastids ; Sequence Homology, Amino Acid ; sitedirected mutagenesis ; Subcellular Fractions - enzymology ; Transferases</subject><ispartof>Chemical and Pharmaceutical Bulletin, 2001, Vol.49(2), pp.197-202</ispartof><rights>2001 The Pharmaceutical Society of Japan</rights><rights>2001 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c623t-733521073578be5ae99e2396dc5902b4711ae1db85332eb0bcaba2dd36839df13</citedby><cites>FETCH-LOGICAL-c623t-733521073578be5ae99e2396dc5902b4711ae1db85332eb0bcaba2dd36839df13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=914138$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11217109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SITTHITHAWORN, Worapan</creatorcontrib><creatorcontrib>KOJIMA, Naoe</creatorcontrib><creatorcontrib>VIROONCHATAPAN, Ekapop</creatorcontrib><creatorcontrib>SUH, Dae-Yeon</creatorcontrib><creatorcontrib>IWANAMI, Naoko</creatorcontrib><creatorcontrib>HAYASHI, Toshimitsu</creatorcontrib><creatorcontrib>NOJI, Masaaki</creatorcontrib><creatorcontrib>SAITO, Kazuki</creatorcontrib><creatorcontrib>NIWA, Yasuo</creatorcontrib><creatorcontrib>SANKAWA, Ushio</creatorcontrib><title>Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis</title><title>Chemical & pharmaceutical bulletin</title><addtitle>Chem. Pharm. Bull.</addtitle><description>cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their N-terminal residues exhibited the characteristics of chloroplast targeting sequence. When expressed in Escherichia coli, both the full-length and truncated proteins in which the putative targeting sequence was deleted catalyzed the condensation of farnesyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate (GGPP). The structural factors determining the product length in plant GGPPSs were investigated by constructing S. dulcis GGPPS mutants on the basis of sequence comparison with the first aspartate-rich motif (FARM) of plant farnesyl diphosphate synthase. The result indicated that in plant GGPPSs small amino acids, Met and Ser, at the fourth and fifth positions before FARM and Pro and Cys insertion in FARM play essential roles in determination of product length. Further, when a chimeric gene comprised of the putative transit peptide of the S. dulcis GGPPS gene and a green fluorescent protein was introduced into Arabidopsis leaves by particle gun bombardment, the chimeric protein was localized in chloroplasts, indicating that the cloned S. dulcis GGPPS is a chloroplast protein.</description><subject>Alkyl and Aryl Transferases - chemistry</subject><subject>Alkyl and Aryl Transferases - genetics</subject><subject>Alkyl and Aryl Transferases - isolation & purification</subject><subject>Alkyl and Aryl Transferases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>cDNA cloning</subject><subject>chloroplast localization</subject><subject>Cloning, Molecular</subject><subject>DNA Primers</subject><subject>DNA, Complementary</subject><subject>Enzymes and enzyme inhibitors</subject><subject>farnesyl diphosphate synthase</subject><subject>Farnesyltranstransferase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>geranylgeranyl diphosphate synthase</subject><subject>Geranyltranstransferase</subject><subject>Magnoliopsida - enzymology</subject><subject>Magnoliopsida - ultrastructure</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>Plastids</subject><subject>Sequence Homology, Amino Acid</subject><subject>sitedirected mutagenesis</subject><subject>Subcellular Fractions - enzymology</subject><subject>Transferases</subject><issn>0009-2363</issn><issn>1347-5223</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kduKFDEQhoMo7uzojQ8gAe-EHnPoU65ERncVRhRWr0Pl0DsZejptkhba9_E9N2OPu954kyLUR31U_Qi9oGRDWdm-0aPalGJDRfMIrSgvm6JijD9GK0KIKBiv-QW6jPFACKtIw5-iC0oZbSgRK_T72gYY5v52Kfi9G_c-jntIFt_MQ9pDtLgL_ohvtB8hOMBm6rWLGAaDt8EnP-A4qX4OkKa4wV97iMkZvPMaevcLksvAH9YPP22Ip2_yGPAVhMHG_ynVjD9PCW5tZlx8hp500Ef7_FzX6PvVh2_bj8Xuy_Wn7btdoWvGU9FwXjGaV6yaVtkKrBCWcVEbXQnCVNlQCpYa1VacM6uI0qCAGcPrlgvTUb5Gr5a5Y_A_JhuTPPgpDFkpaVkTzlibRWv0eqF08DEG28kxuCOEWVIiT4nInIgshcyJZPjleeSkjtY8oOcI_nFCzCfrcg75vPecoCXlbabeLtQhnq5y34aQnO7tXyNbnix-6OwhSDvwO2QXrYg</recordid><startdate>2001</startdate><enddate>2001</enddate><creator>SITTHITHAWORN, Worapan</creator><creator>KOJIMA, Naoe</creator><creator>VIROONCHATAPAN, Ekapop</creator><creator>SUH, Dae-Yeon</creator><creator>IWANAMI, Naoko</creator><creator>HAYASHI, Toshimitsu</creator><creator>NOJI, Masaaki</creator><creator>SAITO, Kazuki</creator><creator>NIWA, Yasuo</creator><creator>SANKAWA, Ushio</creator><general>The Pharmaceutical Society of Japan</general><general>Maruzen</general><general>Japan Science and Technology Agency</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>2001</creationdate><title>Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis</title><author>SITTHITHAWORN, Worapan ; KOJIMA, Naoe ; VIROONCHATAPAN, Ekapop ; SUH, Dae-Yeon ; IWANAMI, Naoko ; HAYASHI, Toshimitsu ; NOJI, Masaaki ; SAITO, Kazuki ; NIWA, Yasuo ; SANKAWA, Ushio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c623t-733521073578be5ae99e2396dc5902b4711ae1db85332eb0bcaba2dd36839df13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Alkyl and Aryl Transferases - chemistry</topic><topic>Alkyl and Aryl Transferases - genetics</topic><topic>Alkyl and Aryl Transferases - isolation & purification</topic><topic>Alkyl and Aryl Transferases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>cDNA cloning</topic><topic>chloroplast localization</topic><topic>Cloning, Molecular</topic><topic>DNA Primers</topic><topic>DNA, Complementary</topic><topic>Enzymes and enzyme inhibitors</topic><topic>farnesyl diphosphate synthase</topic><topic>Farnesyltranstransferase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>geranylgeranyl diphosphate synthase</topic><topic>Geranyltranstransferase</topic><topic>Magnoliopsida - enzymology</topic><topic>Magnoliopsida - ultrastructure</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>Plastids</topic><topic>Sequence Homology, Amino Acid</topic><topic>sitedirected mutagenesis</topic><topic>Subcellular Fractions - enzymology</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SITTHITHAWORN, Worapan</creatorcontrib><creatorcontrib>KOJIMA, Naoe</creatorcontrib><creatorcontrib>VIROONCHATAPAN, Ekapop</creatorcontrib><creatorcontrib>SUH, Dae-Yeon</creatorcontrib><creatorcontrib>IWANAMI, Naoko</creatorcontrib><creatorcontrib>HAYASHI, Toshimitsu</creatorcontrib><creatorcontrib>NOJI, Masaaki</creatorcontrib><creatorcontrib>SAITO, Kazuki</creatorcontrib><creatorcontrib>NIWA, Yasuo</creatorcontrib><creatorcontrib>SANKAWA, Ushio</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Chemical & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SITTHITHAWORN, Worapan</au><au>KOJIMA, Naoe</au><au>VIROONCHATAPAN, Ekapop</au><au>SUH, Dae-Yeon</au><au>IWANAMI, Naoko</au><au>HAYASHI, Toshimitsu</au><au>NOJI, Masaaki</au><au>SAITO, Kazuki</au><au>NIWA, Yasuo</au><au>SANKAWA, Ushio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis</atitle><jtitle>Chemical & pharmaceutical bulletin</jtitle><addtitle>Chem. Pharm. Bull.</addtitle><date>2001</date><risdate>2001</risdate><volume>49</volume><issue>2</issue><spage>197</spage><epage>202</epage><pages>197-202</pages><issn>0009-2363</issn><eissn>1347-5223</eissn><coden>CPBTAL</coden><abstract>cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their N-terminal residues exhibited the characteristics of chloroplast targeting sequence. When expressed in Escherichia coli, both the full-length and truncated proteins in which the putative targeting sequence was deleted catalyzed the condensation of farnesyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate (GGPP). The structural factors determining the product length in plant GGPPSs were investigated by constructing S. dulcis GGPPS mutants on the basis of sequence comparison with the first aspartate-rich motif (FARM) of plant farnesyl diphosphate synthase. The result indicated that in plant GGPPSs small amino acids, Met and Ser, at the fourth and fifth positions before FARM and Pro and Cys insertion in FARM play essential roles in determination of product length. Further, when a chimeric gene comprised of the putative transit peptide of the S. dulcis GGPPS gene and a green fluorescent protein was introduced into Arabidopsis leaves by particle gun bombardment, the chimeric protein was localized in chloroplasts, indicating that the cloned S. dulcis GGPPS is a chloroplast protein.</abstract><cop>Tokyo</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>11217109</pmid><doi>10.1248/cpb.49.197</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Chemical and Pharmaceutical Bulletin, 2001, Vol.49(2), pp.197-202 |
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| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Alkyl and Aryl Transferases - chemistry Alkyl and Aryl Transferases - genetics Alkyl and Aryl Transferases - isolation & purification Alkyl and Aryl Transferases - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences cDNA cloning chloroplast localization Cloning, Molecular DNA Primers DNA, Complementary Enzymes and enzyme inhibitors farnesyl diphosphate synthase Farnesyltranstransferase Fundamental and applied biological sciences. Psychology geranylgeranyl diphosphate synthase Geranyltranstransferase Magnoliopsida - enzymology Magnoliopsida - ultrastructure Molecular Sequence Data Mutagenesis Plastids Sequence Homology, Amino Acid sitedirected mutagenesis Subcellular Fractions - enzymology Transferases |
| title | Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis |
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