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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Veröffentlicht in:Plant physiology (Bethesda) 1995-11, Vol.109 (3), p.999-1006
Hauptverfasser: Knutzon, D.S. (Calgene, Inc., Davis, CA.), Lardizabal, K.D, Nelsen, J.S, Bleibaum, J.L, Davies, H.M, Metz, J.G
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container_title Plant physiology (Bethesda)
container_volume 109
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. 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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&amp;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 &amp; 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. 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(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 &amp; 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. 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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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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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