Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1
The acyl-acyl carrier protein thioesterase B1 from Arabidopsis (AtFATB1) was previously shown to exhibit in vitro hydrolytic activity for long chain acyl-acyl carrier proteins (P. Dörmann, T.A. Voelker, J.B. Ohlrogge [1995] Arch Biochem Biophys 316: 612-618). In this study, we address the question o...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2000-06, Vol.123 (2), p.637-643 |
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| description | The acyl-acyl carrier protein thioesterase B1 from Arabidopsis (AtFATB1) was previously shown to exhibit in vitro hydrolytic activity for long chain acyl-acyl carrier proteins (P. Dörmann, T.A. Voelker, J.B. Ohlrogge [1995] Arch Biochem Biophys 316: 612-618). In this study, we address the question of which role in fatty acid biosynthesis this enzyme plays within the plant. Over-expression of the AtFATB1 cDNA under a seed-specific promoter resulted in accumulation of high amounts of palmitate (16:0) in seeds. RNA and protein-blot analysis in Arabidopsis and rapeseed (Brassica napus) showed that the endogenous AtFATB1 expression was highest in flowers and lower in leaves. All floral tissues of wild-type plants contained elevated amounts of 16:0, and in the polar lipid fraction of flowers close to 50 mol % of the fatty acids were 16:0. Therefore, flowers contain polar lipids with an unusually high amount of saturated fatty acids as compared to all other plant tissues. Antisense expression of the AtFATB1 cDNA under the cauliflower mosaic virus 35S promoter resulted in a reduction of seed and flower 16:0 content, but no changes in leaf fatty acids. We conclude that the AtFATB1 thioesterase contributes to 16:0 production particularly in flowers, but that additional factors are involved in leaves. |
| doi_str_mv | 10.1104/pp.123.2.637 |
| format | Article |
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A ; OHLROGGE, J. B</creator><creatorcontrib>DÖRMANN, P ; VOELKER, T. A ; OHLROGGE, J. B</creatorcontrib><description>The acyl-acyl carrier protein thioesterase B1 from Arabidopsis (AtFATB1) was previously shown to exhibit in vitro hydrolytic activity for long chain acyl-acyl carrier proteins (P. Dörmann, T.A. Voelker, J.B. Ohlrogge [1995] Arch Biochem Biophys 316: 612-618). In this study, we address the question of which role in fatty acid biosynthesis this enzyme plays within the plant. Over-expression of the AtFATB1 cDNA under a seed-specific promoter resulted in accumulation of high amounts of palmitate (16:0) in seeds. RNA and protein-blot analysis in Arabidopsis and rapeseed (Brassica napus) showed that the endogenous AtFATB1 expression was highest in flowers and lower in leaves. All floral tissues of wild-type plants contained elevated amounts of 16:0, and in the polar lipid fraction of flowers close to 50 mol % of the fatty acids were 16:0. Therefore, flowers contain polar lipids with an unusually high amount of saturated fatty acids as compared to all other plant tissues. Antisense expression of the AtFATB1 cDNA under the cauliflower mosaic virus 35S promoter resulted in a reduction of seed and flower 16:0 content, but no changes in leaf fatty acids. We conclude that the AtFATB1 thioesterase contributes to 16:0 production particularly in flowers, but that additional factors are involved in leaves.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.123.2.637</identifier><identifier>PMID: 10859193</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Agronomy. Soil science and plant productions ; Arabidopsis - metabolism ; Arabidopsis Proteins ; Base Sequence ; Biological and medical sciences ; Biosynthesis ; DNA Primers ; Economic plant physiology ; Fatty acids ; Flowers ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Leaves ; Lipid Metabolism ; Lipids ; Metabolism ; Metabolism. Physicochemical requirements ; Nitrogen metabolism and other ones (excepting carbon metabolism) ; Nutrition. Photosynthesis. Respiration. Metabolism ; Palmitic Acid - metabolism ; Plant physiology and development ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plant tissues ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Thiolester Hydrolases - genetics ; Thiolester Hydrolases - metabolism</subject><ispartof>Plant physiology (Bethesda), 2000-06, Vol.123 (2), p.637-643</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright American Society of Plant Physiologists Jun 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-9ebc41bedf3db50eb6dfb517a9ba28e2f8cba85e5504c600839147890cd5df3a3</citedby><cites>FETCH-LOGICAL-c483t-9ebc41bedf3db50eb6dfb517a9ba28e2f8cba85e5504c600839147890cd5df3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1404073$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10859193$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DÖRMANN, P</creatorcontrib><creatorcontrib>VOELKER, T. A</creatorcontrib><creatorcontrib>OHLROGGE, J. B</creatorcontrib><title>Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The acyl-acyl carrier protein thioesterase B1 from Arabidopsis (AtFATB1) was previously shown to exhibit in vitro hydrolytic activity for long chain acyl-acyl carrier proteins (P. Dörmann, T.A. Voelker, J.B. Ohlrogge [1995] Arch Biochem Biophys 316: 612-618). In this study, we address the question of which role in fatty acid biosynthesis this enzyme plays within the plant. Over-expression of the AtFATB1 cDNA under a seed-specific promoter resulted in accumulation of high amounts of palmitate (16:0) in seeds. RNA and protein-blot analysis in Arabidopsis and rapeseed (Brassica napus) showed that the endogenous AtFATB1 expression was highest in flowers and lower in leaves. All floral tissues of wild-type plants contained elevated amounts of 16:0, and in the polar lipid fraction of flowers close to 50 mol % of the fatty acids were 16:0. Therefore, flowers contain polar lipids with an unusually high amount of saturated fatty acids as compared to all other plant tissues. Antisense expression of the AtFATB1 cDNA under the cauliflower mosaic virus 35S promoter resulted in a reduction of seed and flower 16:0 content, but no changes in leaf fatty acids. We conclude that the AtFATB1 thioesterase contributes to 16:0 production particularly in flowers, but that additional factors are involved in leaves.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biosynthesis</subject><subject>DNA Primers</subject><subject>Economic plant physiology</subject><subject>Fatty acids</subject><subject>Flowers</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Leaves</subject><subject>Lipid Metabolism</subject><subject>Lipids</subject><subject>Metabolism</subject><subject>Metabolism. Physicochemical requirements</subject><subject>Nitrogen metabolism and other ones (excepting carbon metabolism)</subject><subject>Nutrition. Photosynthesis. Respiration. Metabolism</subject><subject>Palmitic Acid - metabolism</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plant tissues</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Thiolester Hydrolases - genetics</subject><subject>Thiolester Hydrolases - metabolism</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkElrHDEQRkWwscfLLecgTPDJPS5t09JxYuIFDLk4ZyGpq7FMb5G6D_PvLWcGEnypKopXxccj5CuDNWMgb6dpzbhY8_VG1F_IiinBK66kPiIrgDKD1uaUnOX8BgBMMHlCThloZZgRK4LbEJZ-6dwcx4GOLZ1c18fZzUjjQLfJ-diMU46Z9tjEsm6o39H5FakLu676KDS4lCImOqVxxnI1v8YR84zJZaT325cf7IIct67LeHno5-T3_c-Xu8fq-dfD0932uQpSi7ky6INkHptWNF4B-k3TesVqZ7zjGnmrg3daoVIgwwZAC8NkrQ2ERpUbJ87J9f5vifJnKRlsH3PArnMDjku2NePAjIECXn0C38YlDSWb5UxvuIK_0M0eCmnMOWFrpxR7l3aWgf1wb6fJFveW2-K-4N8OPxdfZP0H72UX4PsBcDm4rk1uCDH_4yRIqIV4B38zjH4</recordid><startdate>20000601</startdate><enddate>20000601</enddate><creator>DÖRMANN, P</creator><creator>VOELKER, T. 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A</au><au>OHLROGGE, J. B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2000-06-01</date><risdate>2000</risdate><volume>123</volume><issue>2</issue><spage>637</spage><epage>643</epage><pages>637-643</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>The acyl-acyl carrier protein thioesterase B1 from Arabidopsis (AtFATB1) was previously shown to exhibit in vitro hydrolytic activity for long chain acyl-acyl carrier proteins (P. Dörmann, T.A. Voelker, J.B. Ohlrogge [1995] Arch Biochem Biophys 316: 612-618). In this study, we address the question of which role in fatty acid biosynthesis this enzyme plays within the plant. Over-expression of the AtFATB1 cDNA under a seed-specific promoter resulted in accumulation of high amounts of palmitate (16:0) in seeds. RNA and protein-blot analysis in Arabidopsis and rapeseed (Brassica napus) showed that the endogenous AtFATB1 expression was highest in flowers and lower in leaves. All floral tissues of wild-type plants contained elevated amounts of 16:0, and in the polar lipid fraction of flowers close to 50 mol % of the fatty acids were 16:0. Therefore, flowers contain polar lipids with an unusually high amount of saturated fatty acids as compared to all other plant tissues. Antisense expression of the AtFATB1 cDNA under the cauliflower mosaic virus 35S promoter resulted in a reduction of seed and flower 16:0 content, but no changes in leaf fatty acids. We conclude that the AtFATB1 thioesterase contributes to 16:0 production particularly in flowers, but that additional factors are involved in leaves.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>10859193</pmid><doi>10.1104/pp.123.2.637</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Agronomy. Soil science and plant productions Arabidopsis - metabolism Arabidopsis Proteins Base Sequence Biological and medical sciences Biosynthesis DNA Primers Economic plant physiology Fatty acids Flowers Fundamental and applied biological sciences. Psychology Gene Expression Leaves Lipid Metabolism Lipids Metabolism Metabolism. Physicochemical requirements Nitrogen metabolism and other ones (excepting carbon metabolism) Nutrition. Photosynthesis. Respiration. Metabolism Palmitic Acid - metabolism Plant physiology and development Plant Proteins - genetics Plant Proteins - metabolism Plant tissues RNA, Messenger - genetics RNA, Messenger - metabolism Thiolester Hydrolases - genetics Thiolester Hydrolases - metabolism |
| title | Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1 |
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