Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates
Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-1- acyl-sn-glycerol-3-phosphate acyltransferase (LPMT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996). Beginning with so...
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creator | Knutzon, D.S. (Calgene, Inc., Davis, CA.) Lardizabal, K.D Nelsen, J.S Bleibaum, J.L Davies, H.M Metz, J.G |
description | Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-1- acyl-sn-glycerol-3-phosphate acyltransferase (LPMT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996). Beginning with solubilized membrane preparations, we have used chromatographic separations to identify a polypeptide with an apparent molecular mass of 29 kD, whose presence in various column fractions correlates with the acyltransferase activity detected in those same fractions. Amino acid sequence data obtained from several peptides generated from this protein were used to isolate a full-length clone from a coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA insert with an open reading frame encoding a 308-amino acid protein with a calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid sequence of pCGN5503 to sequences in the data banks revealed significant homology to other putative LPMT sequences. Expression of the coconut cDNA in Escherichia coli conferred upon those cells a novel LPMT activity whose substrate activity profile matched that of the coconut enzyme |
doi_str_mv | 10.1104/pp.109.3.999 |
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(Calgene, Inc., Davis, CA.) ; Lardizabal, K.D ; Nelsen, J.S ; Bleibaum, J.L ; Davies, H.M ; Metz, J.G</creator><creatorcontrib>Knutzon, D.S. (Calgene, Inc., Davis, CA.) ; Lardizabal, K.D ; Nelsen, J.S ; Bleibaum, J.L ; Davies, H.M ; Metz, J.G</creatorcontrib><description>Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-1- acyl-sn-glycerol-3-phosphate acyltransferase (LPMT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996). Beginning with solubilized membrane preparations, we have used chromatographic separations to identify a polypeptide with an apparent molecular mass of 29 kD, whose presence in various column fractions correlates with the acyltransferase activity detected in those same fractions. Amino acid sequence data obtained from several peptides generated from this protein were used to isolate a full-length clone from a coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA insert with an open reading frame encoding a 308-amino acid protein with a calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid sequence of pCGN5503 to sequences in the data banks revealed significant homology to other putative LPMT sequences. Expression of the coconut cDNA in Escherichia coli conferred upon those cells a novel LPMT activity whose substrate activity profile matched that of the coconut enzyme</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.109.3.999</identifier><identifier>PMID: 8552723</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>1-Acylglycerol-3-Phosphate O-Acyltransferase ; ACIDE GRAS ; ACIDOS GRASOS ; ACILTRANSFERASA ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ACYLTRANSFERASE ; Acyltransferases - genetics ; Acyltransferases - isolation & purification ; Acyltransferases - metabolism ; ADN ; Amino Acid Sequence ; Amino acids ; ARN ; Base Sequence ; Biochemistry and Enzymology ; Biological and medical sciences ; Coconuts ; Cocos - enzymology ; Cocos - genetics ; COCOS NUCIFERA ; Complementary DNA ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DNA Probes ; DNA, Complementary - genetics ; Endosperm ; ENDOSPERMA ; ENDOSPERME ; Enzymes ; ESCHERICHIA COLI ; Escherichia coli - genetics ; Escherichia coli Proteins ; ESTRUCTURA QUIMICA ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fatty acids ; Fundamental and applied biological sciences. Psychology ; Gels ; Gene Library ; MEDIO DE CULTIVO ; Metabolism ; MILIEU DE CULTURE ; Molecular Sequence Data ; Plant physiology and development ; Polymerase Chain Reaction ; PROTEINAS ; PROTEINE ; Proteins ; Recombinant Proteins - metabolism ; RNA ; SECUENCIA NUCLEOTIDICA ; Seeds - enzymology ; Sequence Analysis ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; STRUCTURE CHIMIQUE ; Substrate Specificity ; TECHNIQUE ANALYTIQUE ; TECNICAS ANALITICAS ; TRANSFERENCIA DE GENES ; TRANSFERT DE GENE ; TRIGLICERIDOS ; TRIGLYCERIDE</subject><ispartof>Plant physiology (Bethesda), 1995-11, Vol.109 (3), p.999-1006</ispartof><rights>Copyright 1995 American Society of Plant Physiologists</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-6938a07d052268281eb5953c9542edcd0b7b480d068f62003d9dff827acda7cc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4276892$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4276892$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2916893$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8552723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Knutzon, D.S. (Calgene, Inc., Davis, CA.)</creatorcontrib><creatorcontrib>Lardizabal, K.D</creatorcontrib><creatorcontrib>Nelsen, J.S</creatorcontrib><creatorcontrib>Bleibaum, J.L</creatorcontrib><creatorcontrib>Davies, H.M</creatorcontrib><creatorcontrib>Metz, J.G</creatorcontrib><title>Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-1- acyl-sn-glycerol-3-phosphate acyltransferase (LPMT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996). Beginning with solubilized membrane preparations, we have used chromatographic separations to identify a polypeptide with an apparent molecular mass of 29 kD, whose presence in various column fractions correlates with the acyltransferase activity detected in those same fractions. Amino acid sequence data obtained from several peptides generated from this protein were used to isolate a full-length clone from a coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA insert with an open reading frame encoding a 308-amino acid protein with a calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid sequence of pCGN5503 to sequences in the data banks revealed significant homology to other putative LPMT sequences. Expression of the coconut cDNA in Escherichia coli conferred upon those cells a novel LPMT activity whose substrate activity profile matched that of the coconut enzyme</description><subject>1-Acylglycerol-3-Phosphate O-Acyltransferase</subject><subject>ACIDE GRAS</subject><subject>ACIDOS GRASOS</subject><subject>ACILTRANSFERASA</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ACYLTRANSFERASE</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - isolation & purification</subject><subject>Acyltransferases - metabolism</subject><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>ARN</subject><subject>Base Sequence</subject><subject>Biochemistry and Enzymology</subject><subject>Biological and medical sciences</subject><subject>Coconuts</subject><subject>Cocos - enzymology</subject><subject>Cocos - genetics</subject><subject>COCOS NUCIFERA</subject><subject>Complementary DNA</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DNA Probes</subject><subject>DNA, Complementary - genetics</subject><subject>Endosperm</subject><subject>ENDOSPERMA</subject><subject>ENDOSPERME</subject><subject>Enzymes</subject><subject>ESCHERICHIA COLI</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins</subject><subject>ESTRUCTURA QUIMICA</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fatty acids</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Gene Library</subject><subject>MEDIO DE CULTIVO</subject><subject>Metabolism</subject><subject>MILIEU DE CULTURE</subject><subject>Molecular Sequence Data</subject><subject>Plant physiology and development</subject><subject>Polymerase Chain Reaction</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>Seeds - enzymology</subject><subject>Sequence Analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>STRUCTURE CHIMIQUE</subject><subject>Substrate Specificity</subject><subject>TECHNIQUE ANALYTIQUE</subject><subject>TECNICAS ANALITICAS</subject><subject>TRANSFERENCIA DE GENES</subject><subject>TRANSFERT DE GENE</subject><subject>TRIGLICERIDOS</subject><subject>TRIGLYCERIDE</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU2PFCEQhonRrLOrN09GEw57lJGv7oaDh834mWz0oHsmNNAfmx4gwJjMT_BfS2cmEz1R1PO-VZUqAF4RvCUE8_cxbgmWW7aVUj4BG9IwimjDxVOwwbjGWAj5HFzn_IgxJozwK3AlmoZ2lG3An90S_OxHGAaooQkm-EOBztuQo0t7aD5-v6tfE-wq0pAgbY4Lyh6Ny9G4FBbEUJyqetLFwRWWpH0eXNLZwVKzNWlcLBnunZ0Pe2QmPXu0OD-WCeZDn6uhuPwCPBv0kt3L83sDHj5_-rX7iu5_fPm2u7tHhje0oFYyoXFncUNpK6ggrm9kw4xsOHXWWNx3PRfY4lYMLa0LsNIOg6CdNlZ3xrAb8OFUNx76OpFxvvZfVEzzXqejCnpW_xM_T2oMvxVpCce0-t-d_CaFnJMbLlaC1XoQFWMNpWKqHqTK3_7b7iI-X6Dy2zPX2ehlqMszc77IqCStkKvszUn2mEtIF8xpV_E61OsTHnRQeky1wsNP2ZFq5-wv2yyocA</recordid><startdate>19951101</startdate><enddate>19951101</enddate><creator>Knutzon, D.S. (Calgene, Inc., Davis, CA.)</creator><creator>Lardizabal, K.D</creator><creator>Nelsen, J.S</creator><creator>Bleibaum, J.L</creator><creator>Davies, H.M</creator><creator>Metz, J.G</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><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>5PM</scope></search><sort><creationdate>19951101</creationdate><title>Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates</title><author>Knutzon, D.S. (Calgene, Inc., Davis, CA.) ; Lardizabal, K.D ; Nelsen, J.S ; Bleibaum, J.L ; Davies, H.M ; Metz, J.G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-6938a07d052268281eb5953c9542edcd0b7b480d068f62003d9dff827acda7cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>1-Acylglycerol-3-Phosphate O-Acyltransferase</topic><topic>ACIDE GRAS</topic><topic>ACIDOS GRASOS</topic><topic>ACILTRANSFERASA</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ACYLTRANSFERASE</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - isolation & purification</topic><topic>Acyltransferases - metabolism</topic><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>ARN</topic><topic>Base Sequence</topic><topic>Biochemistry and Enzymology</topic><topic>Biological and medical sciences</topic><topic>Coconuts</topic><topic>Cocos - enzymology</topic><topic>Cocos - genetics</topic><topic>COCOS NUCIFERA</topic><topic>Complementary DNA</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DNA Probes</topic><topic>DNA, Complementary - genetics</topic><topic>Endosperm</topic><topic>ENDOSPERMA</topic><topic>ENDOSPERME</topic><topic>Enzymes</topic><topic>ESCHERICHIA COLI</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins</topic><topic>ESTRUCTURA QUIMICA</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fatty acids</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Gene Library</topic><topic>MEDIO DE CULTIVO</topic><topic>Metabolism</topic><topic>MILIEU DE CULTURE</topic><topic>Molecular Sequence Data</topic><topic>Plant physiology and development</topic><topic>Polymerase Chain Reaction</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>Seeds - enzymology</topic><topic>Sequence Analysis</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><topic>STRUCTURE CHIMIQUE</topic><topic>Substrate Specificity</topic><topic>TECHNIQUE ANALYTIQUE</topic><topic>TECNICAS ANALITICAS</topic><topic>TRANSFERENCIA DE GENES</topic><topic>TRANSFERT DE GENE</topic><topic>TRIGLICERIDOS</topic><topic>TRIGLYCERIDE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Knutzon, D.S. (Calgene, Inc., Davis, CA.)</creatorcontrib><creatorcontrib>Lardizabal, K.D</creatorcontrib><creatorcontrib>Nelsen, J.S</creatorcontrib><creatorcontrib>Bleibaum, J.L</creatorcontrib><creatorcontrib>Davies, H.M</creatorcontrib><creatorcontrib>Metz, J.G</creatorcontrib><collection>AGRIS</collection><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>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Knutzon, D.S. (Calgene, Inc., Davis, CA.)</au><au>Lardizabal, K.D</au><au>Nelsen, J.S</au><au>Bleibaum, J.L</au><au>Davies, H.M</au><au>Metz, J.G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1995-11-01</date><risdate>1995</risdate><volume>109</volume><issue>3</issue><spage>999</spage><epage>1006</epage><pages>999-1006</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Immature coconut (Cocos nucifera) endosperm contains a 1-acyl-1- acyl-sn-glycerol-3-phosphate acyltransferase (LPMT) activity that shows a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M. Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996). Beginning with solubilized membrane preparations, we have used chromatographic separations to identify a polypeptide with an apparent molecular mass of 29 kD, whose presence in various column fractions correlates with the acyltransferase activity detected in those same fractions. Amino acid sequence data obtained from several peptides generated from this protein were used to isolate a full-length clone from a coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA insert with an open reading frame encoding a 308-amino acid protein with a calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid sequence of pCGN5503 to sequences in the data banks revealed significant homology to other putative LPMT sequences. Expression of the coconut cDNA in Escherichia coli conferred upon those cells a novel LPMT activity whose substrate activity profile matched that of the coconut enzyme</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>8552723</pmid><doi>10.1104/pp.109.3.999</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; JSTOR Archive Collection A-Z Listing; Alma/SFX Local Collection |
subjects | 1-Acylglycerol-3-Phosphate O-Acyltransferase ACIDE GRAS ACIDOS GRASOS ACILTRANSFERASA ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ACYLTRANSFERASE Acyltransferases - genetics Acyltransferases - isolation & purification Acyltransferases - metabolism ADN Amino Acid Sequence Amino acids ARN Base Sequence Biochemistry and Enzymology Biological and medical sciences Coconuts Cocos - enzymology Cocos - genetics COCOS NUCIFERA Complementary DNA COMPOSICION QUIMICA COMPOSITION CHIMIQUE DNA Probes DNA, Complementary - genetics Endosperm ENDOSPERMA ENDOSPERME Enzymes ESCHERICHIA COLI Escherichia coli - genetics Escherichia coli Proteins ESTRUCTURA QUIMICA EXPRESION GENICA EXPRESSION DES GENES Fatty acids Fundamental and applied biological sciences. Psychology Gels Gene Library MEDIO DE CULTIVO Metabolism MILIEU DE CULTURE Molecular Sequence Data Plant physiology and development Polymerase Chain Reaction PROTEINAS PROTEINE Proteins Recombinant Proteins - metabolism RNA SECUENCIA NUCLEOTIDICA Seeds - enzymology Sequence Analysis Sequence Homology, Amino Acid SEQUENCE NUCLEOTIDIQUE STRUCTURE CHIMIQUE Substrate Specificity TECHNIQUE ANALYTIQUE TECNICAS ANALITICAS TRANSFERENCIA DE GENES TRANSFERT DE GENE TRIGLICERIDOS TRIGLYCERIDE |
title | Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates |
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