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Involvement of the Phospholipid Sterol Acyltransferase1 in Plant Sterol Homeostasis and Leaf Senescence
Genes encoding sterol ester-forming enzymes were recently identified in the Arabidopsis (Arabidopsis thaliana) genome. One belongs to a family of six members presenting homologies with the mammalian Lecithin Cholesterol Acyltransferases. The other one belongs to the superfamily of Membrane-Bound O-A...
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Published in: | Plant physiology (Bethesda) 2010-01, Vol.152 (1), p.107-119 |
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description | Genes encoding sterol ester-forming enzymes were recently identified in the Arabidopsis (Arabidopsis thaliana) genome. One belongs to a family of six members presenting homologies with the mammalian Lecithin Cholesterol Acyltransferases. The other one belongs to the superfamily of Membrane-Bound O-Acyltransferases. The physiological functions of these genes, Phospholipid Sterol Acyltransferase1 (PSAT1) and Acyl-CoA Sterol Acyltransferase1 (ASAT1), respectively, were investigated using Arabidopsis mutants. Sterol ester content decreased in leaves of all mutants and was strongly reduced in seeds from plants carrying a PSAT1-deficient mutation. The amount of sterol esters in flowers was very close to that of the wild type for all lines studied. This indicated further functional redundancy of sterol acylation in Arabidopsis. We performed feeding experiments in which we supplied sterol precursors to psat1-1, psat1-2, and asat1-1 mutants. This triggered the accumulation of sterol esters (stored in cytosolic lipid droplets) in the wild type and the asat1-1 lines but not in the psat1-1 and psat1-2 lines, indicating a major contribution of the PSAT1 in maintaining free sterol homeostasis in plant cell membranes. A clear biological effect associated with the lack of sterol ester formation in the psat1-1 and psat1-2 mutants was an early leaf senescence phenotype. Double mutants lacking PSAT1 and ASAT1 had identical phenotypes to psat1 mutants. The results presented here suggest that PSAT1 plays a role in lipid catabolism as part of the intracellular processes at play in the maintenance of leaf viability during developmental aging. |
doi_str_mv | 10.1104/pp.109.145672 |
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One belongs to a family of six members presenting homologies with the mammalian Lecithin Cholesterol Acyltransferases. The other one belongs to the superfamily of Membrane-Bound O-Acyltransferases. The physiological functions of these genes, Phospholipid Sterol Acyltransferase1 (PSAT1) and Acyl-CoA Sterol Acyltransferase1 (ASAT1), respectively, were investigated using Arabidopsis mutants. Sterol ester content decreased in leaves of all mutants and was strongly reduced in seeds from plants carrying a PSAT1-deficient mutation. The amount of sterol esters in flowers was very close to that of the wild type for all lines studied. This indicated further functional redundancy of sterol acylation in Arabidopsis. We performed feeding experiments in which we supplied sterol precursors to psat1-1, psat1-2, and asat1-1 mutants. This triggered the accumulation of sterol esters (stored in cytosolic lipid droplets) in the wild type and the asat1-1 lines but not in the psat1-1 and psat1-2 lines, indicating a major contribution of the PSAT1 in maintaining free sterol homeostasis in plant cell membranes. A clear biological effect associated with the lack of sterol ester formation in the psat1-1 and psat1-2 mutants was an early leaf senescence phenotype. Double mutants lacking PSAT1 and ASAT1 had identical phenotypes to psat1 mutants. 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One belongs to a family of six members presenting homologies with the mammalian Lecithin Cholesterol Acyltransferases. The other one belongs to the superfamily of Membrane-Bound O-Acyltransferases. The physiological functions of these genes, Phospholipid Sterol Acyltransferase1 (PSAT1) and Acyl-CoA Sterol Acyltransferase1 (ASAT1), respectively, were investigated using Arabidopsis mutants. Sterol ester content decreased in leaves of all mutants and was strongly reduced in seeds from plants carrying a PSAT1-deficient mutation. The amount of sterol esters in flowers was very close to that of the wild type for all lines studied. This indicated further functional redundancy of sterol acylation in Arabidopsis. We performed feeding experiments in which we supplied sterol precursors to psat1-1, psat1-2, and asat1-1 mutants. This triggered the accumulation of sterol esters (stored in cytosolic lipid droplets) in the wild type and the asat1-1 lines but not in the psat1-1 and psat1-2 lines, indicating a major contribution of the PSAT1 in maintaining free sterol homeostasis in plant cell membranes. A clear biological effect associated with the lack of sterol ester formation in the psat1-1 and psat1-2 mutants was an early leaf senescence phenotype. Double mutants lacking PSAT1 and ASAT1 had identical phenotypes to psat1 mutants. The results presented here suggest that PSAT1 plays a role in lipid catabolism as part of the intracellular processes at play in the maintenance of leaf viability during developmental aging.</description><subject>Agricultural Science</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES</subject><subject>Cellular Biology</subject><subject>Cellular senescence</subject><subject>Enzymes</subject><subject>Esters</subject><subject>Flowers - enzymology</subject><subject>Homeostasis</subject><subject>Horticulture</subject><subject>Jordbruksvetenskap</subject><subject>Leaves</subject><subject>Life Sciences</subject><subject>Lipids</subject><subject>Mevalonic Acid - analogs & derivatives</subject><subject>Mutagenesis, Insertional</subject><subject>Mutation</subject><subject>Phenotypes</subject><subject>Phytosterols - metabolism</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Leaves - physiology</subject><subject>Plants</subject><subject>Seeds</subject><subject>Seeds - enzymology</subject><subject>Squalene</subject><subject>Sterols</subject><subject>Trädgårdsvetenskap/hortikultur</subject><issn>0032-0889</issn><issn>1532-2548</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNpdks9r2zAUx8XYWLNsxx236dqDM_22dBmEsi6FwApZz0K2n2IXxzKSm9L_fgoO7brTe-j7-X71xBNCnylZUUrE93FcUWJWVEhVsjdoQSVnBZNCv0ULQnJPtDYX6ENK94QQyql4jy6oMYwzbhZofzMcQ3-EAwwTDh5PLeDbNqSxDX03dg3eTRBDj9f1Uz9FNyQP0SWguBvwbe-y6QxswgFCmlzqEnZDg7fgPN7BAKmGoYaP6J13fYJP57pEd9c__1xtiu3vXzdX621RK6KmQkqjGNfOK1NWsm7AVGVplK6Fqgw0noKotNBSq7qslWJeSSUaXQlJGeHe8CUq5tz0CONDZcfYHVx8ssF1NvUPlYunYhNYRaQuM_9j5jN8gCbPml_Zv7K9VoautftwtKw0hkuSAy7ngPY_22a9taczQoTkgqsjfRmujiGlCP7ZQIk9bdOOY26NnbeZ-a__DvdCn9eXgS8zcJ-mEJ91JpUmKl-6RN9m3btg3T52yd7tWP4FhJaMSGH4X9cZr3o</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Bouvier-Navé, Pierrette</creator><creator>Berna, Anne</creator><creator>Noiriel, Alexandre</creator><creator>Compagnon, Vincent</creator><creator>Carlsson, Anders S</creator><creator>Banas, Antoni</creator><creator>Stymne, Sten</creator><creator>Schaller, Hubert</creator><general>American Society of Plant Biologists</general><general>Oxford University Press ; American Society of Plant Biologists</general><scope>FBQ</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>1XC</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid></search><sort><creationdate>20100101</creationdate><title>Involvement of the Phospholipid Sterol Acyltransferase1 in Plant Sterol Homeostasis and Leaf Senescence</title><author>Bouvier-Navé, Pierrette ; Berna, Anne ; Noiriel, Alexandre ; Compagnon, Vincent ; Carlsson, Anders S ; Banas, Antoni ; Stymne, Sten ; Schaller, Hubert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c606t-5596238af697b5cde9b77968c46b9edf1e4b848586c7c662f6564d8b451203f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Agricultural Science</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES</topic><topic>Cellular Biology</topic><topic>Cellular senescence</topic><topic>Enzymes</topic><topic>Esters</topic><topic>Flowers - enzymology</topic><topic>Homeostasis</topic><topic>Horticulture</topic><topic>Jordbruksvetenskap</topic><topic>Leaves</topic><topic>Life Sciences</topic><topic>Lipids</topic><topic>Mevalonic Acid - analogs & derivatives</topic><topic>Mutagenesis, Insertional</topic><topic>Mutation</topic><topic>Phenotypes</topic><topic>Phytosterols - metabolism</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Leaves - physiology</topic><topic>Plants</topic><topic>Seeds</topic><topic>Seeds - enzymology</topic><topic>Squalene</topic><topic>Sterols</topic><topic>Trädgårdsvetenskap/hortikultur</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bouvier-Navé, Pierrette</creatorcontrib><creatorcontrib>Berna, Anne</creatorcontrib><creatorcontrib>Noiriel, Alexandre</creatorcontrib><creatorcontrib>Compagnon, Vincent</creatorcontrib><creatorcontrib>Carlsson, Anders S</creatorcontrib><creatorcontrib>Banas, Antoni</creatorcontrib><creatorcontrib>Stymne, Sten</creatorcontrib><creatorcontrib>Schaller, Hubert</creatorcontrib><creatorcontrib>Sveriges lantbruksuniversitet</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bouvier-Navé, Pierrette</au><au>Berna, Anne</au><au>Noiriel, Alexandre</au><au>Compagnon, Vincent</au><au>Carlsson, Anders S</au><au>Banas, Antoni</au><au>Stymne, Sten</au><au>Schaller, Hubert</au><aucorp>Sveriges lantbruksuniversitet</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of the Phospholipid Sterol Acyltransferase1 in Plant Sterol Homeostasis and Leaf Senescence</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2010-01-01</date><risdate>2010</risdate><volume>152</volume><issue>1</issue><spage>107</spage><epage>119</epage><pages>107-119</pages><issn>0032-0889</issn><issn>1532-2548</issn><eissn>1532-2548</eissn><abstract>Genes encoding sterol ester-forming enzymes were recently identified in the Arabidopsis (Arabidopsis thaliana) genome. One belongs to a family of six members presenting homologies with the mammalian Lecithin Cholesterol Acyltransferases. The other one belongs to the superfamily of Membrane-Bound O-Acyltransferases. The physiological functions of these genes, Phospholipid Sterol Acyltransferase1 (PSAT1) and Acyl-CoA Sterol Acyltransferase1 (ASAT1), respectively, were investigated using Arabidopsis mutants. Sterol ester content decreased in leaves of all mutants and was strongly reduced in seeds from plants carrying a PSAT1-deficient mutation. The amount of sterol esters in flowers was very close to that of the wild type for all lines studied. This indicated further functional redundancy of sterol acylation in Arabidopsis. We performed feeding experiments in which we supplied sterol precursors to psat1-1, psat1-2, and asat1-1 mutants. This triggered the accumulation of sterol esters (stored in cytosolic lipid droplets) in the wild type and the asat1-1 lines but not in the psat1-1 and psat1-2 lines, indicating a major contribution of the PSAT1 in maintaining free sterol homeostasis in plant cell membranes. A clear biological effect associated with the lack of sterol ester formation in the psat1-1 and psat1-2 mutants was an early leaf senescence phenotype. Double mutants lacking PSAT1 and ASAT1 had identical phenotypes to psat1 mutants. The results presented here suggest that PSAT1 plays a role in lipid catabolism as part of the intracellular processes at play in the maintenance of leaf viability during developmental aging.</abstract><cop>United States</cop><pub>American Society of Plant Biologists</pub><pmid>19923239</pmid><doi>10.1104/pp.109.145672</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Agricultural Science Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES Cellular Biology Cellular senescence Enzymes Esters Flowers - enzymology Homeostasis Horticulture Jordbruksvetenskap Leaves Life Sciences Lipids Mevalonic Acid - analogs & derivatives Mutagenesis, Insertional Mutation Phenotypes Phytosterols - metabolism Plant Leaves - enzymology Plant Leaves - physiology Plants Seeds Seeds - enzymology Squalene Sterols Trädgårdsvetenskap/hortikultur |
title | Involvement of the Phospholipid Sterol Acyltransferase1 in Plant Sterol Homeostasis and Leaf Senescence |
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