Palmitoyl-Acyl Carrier Protein (ACP) Thioesterase and the Evolutionary Origin of Plant Acyl-ACP Thioesterases
Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene class...
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| Veröffentlicht in: | The Plant cell 1995-03, Vol.7 (3), p.359-371 |
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| container_title | The Plant cell |
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| creator | Jones, Aubrey Davies, H. Maelor Voelker, Toni A. |
| description | Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene classes in higher plants, termed FatA and FatB, whose evolutionary divergence appears to be ancient. FatA encodes the already described 18:1-ACP thioesterase. In contrast, FatB representatives encode thioesterases preferring acyl-ACPs having saturated acyl groups. We unexpectedly obtained a 16:0-ACP thioesterase cDNA from Cuphea hookeriana seed, which accumulate predominantly 8:0 and 10:0. The 16:0 thioesterase transcripts were found in non-seed tissues, and expression in transgenic Brassica napus led to the production of a 16:0-rich oil. We present evidence that this type of FatB gene is ancient and ubiquitous in plants and that specialized plant medium-chain thioesterases have evolved independently from such enzymes several times during angiosperm evolution. Also, the ubiquitous 18:1-ACP thioesterase appears to be a derivative of a 16:0 thioesterase. |
| doi_str_mv | 10.1105/tpc.7.3.359 |
| format | Article |
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Maelor ; Voelker, Toni A.</creator><creatorcontrib>Jones, Aubrey ; Davies, H. Maelor ; Voelker, Toni A.</creatorcontrib><description>Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene classes in higher plants, termed FatA and FatB, whose evolutionary divergence appears to be ancient. FatA encodes the already described 18:1-ACP thioesterase. In contrast, FatB representatives encode thioesterases preferring acyl-ACPs having saturated acyl groups. We unexpectedly obtained a 16:0-ACP thioesterase cDNA from Cuphea hookeriana seed, which accumulate predominantly 8:0 and 10:0. The 16:0 thioesterase transcripts were found in non-seed tissues, and expression in transgenic Brassica napus led to the production of a 16:0-rich oil. We present evidence that this type of FatB gene is ancient and ubiquitous in plants and that specialized plant medium-chain thioesterases have evolved independently from such enzymes several times during angiosperm evolution. Also, the ubiquitous 18:1-ACP thioesterase appears to be a derivative of a 16:0 thioesterase.</description><identifier>ISSN: 1040-4651</identifier><identifier>EISSN: 1532-298X</identifier><identifier>DOI: 10.1105/tpc.7.3.359</identifier><identifier>PMID: 7734968</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>Amino Acid Sequence ; Amino acids ; Base Sequence ; Biological Evolution ; Complementary DNA ; DNA Primers ; DNA, Complementary ; DNA, Plant - metabolism ; Enzymes ; Evolution ; Fatty acids ; Lipids ; Molecular Sequence Data ; Phylogeny ; Plant cells ; Plants ; Plants - enzymology ; Plants - genetics ; Polymerase Chain Reaction ; RNA, Plant - isolation & purification ; RNA, Plant - metabolism ; Seeds ; Sequence Homology, Amino Acid ; Thiolester Hydrolases - chemistry ; Thiolester Hydrolases - genetics ; Thiolester Hydrolases - metabolism</subject><ispartof>The Plant cell, 1995-03, Vol.7 (3), p.359-371</ispartof><rights>Copyright 1995 American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-e49741f7c6fd44d319485173498b02a225a03f7e532229ac187d321bcdd71d393</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3869857$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3869857$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7734968$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jones, Aubrey</creatorcontrib><creatorcontrib>Davies, H. Maelor</creatorcontrib><creatorcontrib>Voelker, Toni A.</creatorcontrib><title>Palmitoyl-Acyl Carrier Protein (ACP) Thioesterase and the Evolutionary Origin of Plant Acyl-ACP Thioesterases</title><title>The Plant cell</title><addtitle>Plant Cell</addtitle><description>Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene classes in higher plants, termed FatA and FatB, whose evolutionary divergence appears to be ancient. FatA encodes the already described 18:1-ACP thioesterase. In contrast, FatB representatives encode thioesterases preferring acyl-ACPs having saturated acyl groups. We unexpectedly obtained a 16:0-ACP thioesterase cDNA from Cuphea hookeriana seed, which accumulate predominantly 8:0 and 10:0. The 16:0 thioesterase transcripts were found in non-seed tissues, and expression in transgenic Brassica napus led to the production of a 16:0-rich oil. We present evidence that this type of FatB gene is ancient and ubiquitous in plants and that specialized plant medium-chain thioesterases have evolved independently from such enzymes several times during angiosperm evolution. Also, the ubiquitous 18:1-ACP thioesterase appears to be a derivative of a 16:0 thioesterase.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Biological Evolution</subject><subject>Complementary DNA</subject><subject>DNA Primers</subject><subject>DNA, Complementary</subject><subject>DNA, Plant - metabolism</subject><subject>Enzymes</subject><subject>Evolution</subject><subject>Fatty acids</subject><subject>Lipids</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Plant cells</subject><subject>Plants</subject><subject>Plants - enzymology</subject><subject>Plants - genetics</subject><subject>Polymerase Chain Reaction</subject><subject>RNA, Plant - isolation & purification</subject><subject>RNA, Plant - metabolism</subject><subject>Seeds</subject><subject>Sequence Homology, Amino Acid</subject><subject>Thiolester Hydrolases - chemistry</subject><subject>Thiolester Hydrolases - genetics</subject><subject>Thiolester Hydrolases - metabolism</subject><issn>1040-4651</issn><issn>1532-298X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUctKAzEUDaL4XrkWshBRZGpeM0kWLkrxBYV2oeAupJmMjcxMapIW-vemtIiu7oXzuOdyALjAaIAxKu_Twgz4gA5oKffAMS4pKYgUH_t5RwwVrCrxETiJ8QshhDmWh-CQc8pkJY5BN9Vt55Jft8XQrFs40iE4G-A0-GRdD2-Go-ktfJs7b2OyQUcLdV_DNLfwceXbZXK-12ENJ8F9Zrpv4LTVfYIbsyJr_0njGThodBvt-W6egvenx7fRSzGePL-OhuPCMFqmwjLJGW64qZqasZpiyUSJN5HFDBFNSKkRbbjNnxIitcGC15Tgmalrjmsq6Sl42PoulrPO1sb2KehWLYLrcljltVP_kd7N1adfKVwhLkTWX-_0wX8vc3zVuWhsm1-zfhkV54QRLHkm3m2JJvgYg21-b2CkNuWoXI7iiqpcTmZf_o31y921kfGrLf4Vkw9_rQhF2URUUpSc_gDhDpca</recordid><startdate>19950301</startdate><enddate>19950301</enddate><creator>Jones, Aubrey</creator><creator>Davies, H. Maelor</creator><creator>Voelker, Toni A.</creator><general>American Society of Plant Physiologists</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950301</creationdate><title>Palmitoyl-Acyl Carrier Protein (ACP) Thioesterase and the Evolutionary Origin of Plant Acyl-ACP Thioesterases</title><author>Jones, Aubrey ; Davies, H. Maelor ; Voelker, Toni A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-e49741f7c6fd44d319485173498b02a225a03f7e532229ac187d321bcdd71d393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Base Sequence</topic><topic>Biological Evolution</topic><topic>Complementary DNA</topic><topic>DNA Primers</topic><topic>DNA, Complementary</topic><topic>DNA, Plant - metabolism</topic><topic>Enzymes</topic><topic>Evolution</topic><topic>Fatty acids</topic><topic>Lipids</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Plant cells</topic><topic>Plants</topic><topic>Plants - enzymology</topic><topic>Plants - genetics</topic><topic>Polymerase Chain Reaction</topic><topic>RNA, Plant - isolation & purification</topic><topic>RNA, Plant - metabolism</topic><topic>Seeds</topic><topic>Sequence Homology, Amino Acid</topic><topic>Thiolester Hydrolases - chemistry</topic><topic>Thiolester Hydrolases - genetics</topic><topic>Thiolester Hydrolases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jones, Aubrey</creatorcontrib><creatorcontrib>Davies, H. Maelor</creatorcontrib><creatorcontrib>Voelker, Toni A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Plant cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jones, Aubrey</au><au>Davies, H. Maelor</au><au>Voelker, Toni A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Palmitoyl-Acyl Carrier Protein (ACP) Thioesterase and the Evolutionary Origin of Plant Acyl-ACP Thioesterases</atitle><jtitle>The Plant cell</jtitle><addtitle>Plant Cell</addtitle><date>1995-03-01</date><risdate>1995</risdate><volume>7</volume><issue>3</issue><spage>359</spage><epage>371</epage><pages>359-371</pages><issn>1040-4651</issn><eissn>1532-298X</eissn><abstract>Acyl-acyl carrier protein (ACP) thioesterases play an essential role in chain termination during de novo fatty acid synthesis and in the channeling of carbon flux between the two lipid biosynthesis pathways in plants. We have discovered that there are two distinct but related thioesterase gene classes in higher plants, termed FatA and FatB, whose evolutionary divergence appears to be ancient. FatA encodes the already described 18:1-ACP thioesterase. In contrast, FatB representatives encode thioesterases preferring acyl-ACPs having saturated acyl groups. We unexpectedly obtained a 16:0-ACP thioesterase cDNA from Cuphea hookeriana seed, which accumulate predominantly 8:0 and 10:0. The 16:0 thioesterase transcripts were found in non-seed tissues, and expression in transgenic Brassica napus led to the production of a 16:0-rich oil. We present evidence that this type of FatB gene is ancient and ubiquitous in plants and that specialized plant medium-chain thioesterases have evolved independently from such enzymes several times during angiosperm evolution. Also, the ubiquitous 18:1-ACP thioesterase appears to be a derivative of a 16:0 thioesterase.</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>7734968</pmid><doi>10.1105/tpc.7.3.359</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Plant cell, 1995-03, Vol.7 (3), p.359-371 |
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| language | eng |
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| source | Jstor Complete Legacy; MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino acids Base Sequence Biological Evolution Complementary DNA DNA Primers DNA, Complementary DNA, Plant - metabolism Enzymes Evolution Fatty acids Lipids Molecular Sequence Data Phylogeny Plant cells Plants Plants - enzymology Plants - genetics Polymerase Chain Reaction RNA, Plant - isolation & purification RNA, Plant - metabolism Seeds Sequence Homology, Amino Acid Thiolester Hydrolases - chemistry Thiolester Hydrolases - genetics Thiolester Hydrolases - metabolism |
| title | Palmitoyl-Acyl Carrier Protein (ACP) Thioesterase and the Evolutionary Origin of Plant Acyl-ACP Thioesterases |
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