Oil and Protein Accumulation in Developing Seeds Is Influenced by the Expression of a Cytosolic Pyrophosphatase in Arabidopsis
This study describes a dominant low-seed-oil mutant (lo15571) of Arabidopsis (Arabidopsis thaliana) generated by enhancer tagging. Compositional analysis of developing siliques and mature seeds indicated reduced conversion of photoassimilates to oil. Immunoblot analysis revealed increased levels of...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2012-07, Vol.159 (3), p.1221-1234 |
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| creator | Meyer, Knut Stecca, Kevin L. Ewell-Hicks, Kim Allen, Stephen M. Everard, John D. |
| description | This study describes a dominant low-seed-oil mutant (lo15571) of Arabidopsis (Arabidopsis thaliana) generated by enhancer tagging. Compositional analysis of developing siliques and mature seeds indicated reduced conversion of photoassimilates to oil. Immunoblot analysis revealed increased levels of At1g01050 protein in developing siliques of lo15571. At1g01050 encodes a soluble, cytosolic pyrophosphatase and is one of five closely related genes that share predicted cytosolic localization and at least 70% amino acid sequence identity. Expression of At1g01050 using a seed-preferred promoter recreated most features of the lo15571 seed phenotype, including low seed oil content and increased levels of transient starch and soluble sugars in developing siliques. Seed-preferred RNA interference-mediated silencing of Atlg01050 and At3g53620, a second cytosolic pyrophosphatase gene that shows expression during seed filling, led to a heritable oil increase of 1% to 4%, mostly at the expense of seed storage protein. These results are consistent with a scenario in which the rate of mobilization of sucrose, for precursor supply of seed storage lipid biosynthesis by cytosolic glycolysis, is strongly influenced by the expression of endogenous pyrophosphatase enzymes. This emphasizes the central role of pyrophosphate-dependent reactions supporting cytosolic glycolysis during seed maturation when ATP supply is low, presumably due to hypoxic conditions. This route is the major route providing precursors for seed oil biosynthesis. ATP-dependent reactions at the entry point of glycolysis in the cytosol or plastid cannot fully compensate for the loss of oil content observed in transgenic events with increased expression of cytosolic pyrophosphatase enzyme in the cytosol. These findings shed new light on the dynamic properties of cytosolic pyrophosphate pools in developing seed and their influence on carbon partitioning during seed filling. Finally, our work uniquely demonstrates that genes encoding cytosolic pyrophosphatase enzymes provide novel targets to improve seed composition for plant biotechnology applications. |
| doi_str_mv | 10.1104/pp.112.198309 |
| format | Article |
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Compositional analysis of developing siliques and mature seeds indicated reduced conversion of photoassimilates to oil. Immunoblot analysis revealed increased levels of At1g01050 protein in developing siliques of lo15571. At1g01050 encodes a soluble, cytosolic pyrophosphatase and is one of five closely related genes that share predicted cytosolic localization and at least 70% amino acid sequence identity. Expression of At1g01050 using a seed-preferred promoter recreated most features of the lo15571 seed phenotype, including low seed oil content and increased levels of transient starch and soluble sugars in developing siliques. Seed-preferred RNA interference-mediated silencing of Atlg01050 and At3g53620, a second cytosolic pyrophosphatase gene that shows expression during seed filling, led to a heritable oil increase of 1% to 4%, mostly at the expense of seed storage protein. These results are consistent with a scenario in which the rate of mobilization of sucrose, for precursor supply of seed storage lipid biosynthesis by cytosolic glycolysis, is strongly influenced by the expression of endogenous pyrophosphatase enzymes. This emphasizes the central role of pyrophosphate-dependent reactions supporting cytosolic glycolysis during seed maturation when ATP supply is low, presumably due to hypoxic conditions. This route is the major route providing precursors for seed oil biosynthesis. ATP-dependent reactions at the entry point of glycolysis in the cytosol or plastid cannot fully compensate for the loss of oil content observed in transgenic events with increased expression of cytosolic pyrophosphatase enzyme in the cytosol. These findings shed new light on the dynamic properties of cytosolic pyrophosphate pools in developing seed and their influence on carbon partitioning during seed filling. Finally, our work uniquely demonstrates that genes encoding cytosolic pyrophosphatase enzymes provide novel targets to improve seed composition for plant biotechnology applications.</description><identifier>ISSN: 0032-0889</identifier><identifier>ISSN: 1532-2548</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.112.198309</identifier><identifier>PMID: 22566496</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>adenosine triphosphate ; amino acid sequences ; Amino acids ; anaerobic conditions ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - growth & development ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; ATP ; BIOCHEMICAL PROCESS AND MACROMOLECULAR STRUCTURES ; Biochemical Processes and Macromolecular Structures ; Biological and medical sciences ; Biosynthesis ; Biotechnology ; carbon ; Centrifugation, Density Gradient ; Crosses, Genetic ; cytosol ; Cytosol - enzymology ; Enzymes ; filling period ; fruits ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant ; genes ; Genes, Dominant - genetics ; Genes, Plant - genetics ; Genetic Association Studies ; genetically modified organisms ; Glycolysis ; Hypoxia ; Immunoblotting ; lipid content ; lipids ; Models, Biological ; Mutagenesis, Insertional - genetics ; mutants ; Mutation - genetics ; Oils & fats ; phenotype ; Phenotypes ; Phylogeny ; Plant Oils - metabolism ; Plant physiology and development ; Plants ; Plants, Genetically Modified ; Pyrophosphatases - genetics ; Pyrophosphatases - metabolism ; Reproducibility of Results ; RNA ; RNA Interference ; Seed maturation ; seed oils ; Seed storage ; Seeds ; Seeds - growth & development ; Seeds - metabolism ; sequence analysis ; starch ; Starches ; sucrose ; Sugars</subject><ispartof>Plant physiology (Bethesda), 2012-07, Vol.159 (3), p.1221-1234</ispartof><rights>2012 American Society of Plant Biologists</rights><rights>2015 INIST-CNRS</rights><rights>Copyright American Society of Plant Biologists Jul 2012</rights><rights>2012 American Society of Plant Biologists. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c566t-ab1d131742018b2d1d2a8bfb77f7d77b641b055367ed44a9bfb69e46e7b02b7d3</citedby><cites>FETCH-LOGICAL-c566t-ab1d131742018b2d1d2a8bfb77f7d77b641b055367ed44a9bfb69e46e7b02b7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41549935$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41549935$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26144820$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22566496$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meyer, Knut</creatorcontrib><creatorcontrib>Stecca, Kevin L.</creatorcontrib><creatorcontrib>Ewell-Hicks, Kim</creatorcontrib><creatorcontrib>Allen, Stephen M.</creatorcontrib><creatorcontrib>Everard, John D.</creatorcontrib><title>Oil and Protein Accumulation in Developing Seeds Is Influenced by the Expression of a Cytosolic Pyrophosphatase in Arabidopsis</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>This study describes a dominant low-seed-oil mutant (lo15571) of Arabidopsis (Arabidopsis thaliana) generated by enhancer tagging. Compositional analysis of developing siliques and mature seeds indicated reduced conversion of photoassimilates to oil. Immunoblot analysis revealed increased levels of At1g01050 protein in developing siliques of lo15571. At1g01050 encodes a soluble, cytosolic pyrophosphatase and is one of five closely related genes that share predicted cytosolic localization and at least 70% amino acid sequence identity. Expression of At1g01050 using a seed-preferred promoter recreated most features of the lo15571 seed phenotype, including low seed oil content and increased levels of transient starch and soluble sugars in developing siliques. Seed-preferred RNA interference-mediated silencing of Atlg01050 and At3g53620, a second cytosolic pyrophosphatase gene that shows expression during seed filling, led to a heritable oil increase of 1% to 4%, mostly at the expense of seed storage protein. These results are consistent with a scenario in which the rate of mobilization of sucrose, for precursor supply of seed storage lipid biosynthesis by cytosolic glycolysis, is strongly influenced by the expression of endogenous pyrophosphatase enzymes. This emphasizes the central role of pyrophosphate-dependent reactions supporting cytosolic glycolysis during seed maturation when ATP supply is low, presumably due to hypoxic conditions. This route is the major route providing precursors for seed oil biosynthesis. ATP-dependent reactions at the entry point of glycolysis in the cytosol or plastid cannot fully compensate for the loss of oil content observed in transgenic events with increased expression of cytosolic pyrophosphatase enzyme in the cytosol. These findings shed new light on the dynamic properties of cytosolic pyrophosphate pools in developing seed and their influence on carbon partitioning during seed filling. Finally, our work uniquely demonstrates that genes encoding cytosolic pyrophosphatase enzymes provide novel targets to improve seed composition for plant biotechnology applications.</description><subject>adenosine triphosphate</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>anaerobic conditions</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - growth & development</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>ATP</subject><subject>BIOCHEMICAL PROCESS AND MACROMOLECULAR STRUCTURES</subject><subject>Biochemical Processes and Macromolecular Structures</subject><subject>Biological and medical sciences</subject><subject>Biosynthesis</subject><subject>Biotechnology</subject><subject>carbon</subject><subject>Centrifugation, Density Gradient</subject><subject>Crosses, Genetic</subject><subject>cytosol</subject><subject>Cytosol - enzymology</subject><subject>Enzymes</subject><subject>filling period</subject><subject>fruits</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Plant</subject><subject>genes</subject><subject>Genes, Dominant - genetics</subject><subject>Genes, Plant - genetics</subject><subject>Genetic Association Studies</subject><subject>genetically modified organisms</subject><subject>Glycolysis</subject><subject>Hypoxia</subject><subject>Immunoblotting</subject><subject>lipid content</subject><subject>lipids</subject><subject>Models, Biological</subject><subject>Mutagenesis, Insertional - genetics</subject><subject>mutants</subject><subject>Mutation - genetics</subject><subject>Oils & fats</subject><subject>phenotype</subject><subject>Phenotypes</subject><subject>Phylogeny</subject><subject>Plant Oils - metabolism</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>Plants, Genetically Modified</subject><subject>Pyrophosphatases - genetics</subject><subject>Pyrophosphatases - metabolism</subject><subject>Reproducibility of Results</subject><subject>RNA</subject><subject>RNA Interference</subject><subject>Seed maturation</subject><subject>seed oils</subject><subject>Seed storage</subject><subject>Seeds</subject><subject>Seeds - growth & development</subject><subject>Seeds - metabolism</subject><subject>sequence analysis</subject><subject>starch</subject><subject>Starches</subject><subject>sucrose</subject><subject>Sugars</subject><issn>0032-0889</issn><issn>1532-2548</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkd1rFDEUxYModq0--qgERPBlapLJJDMvhWWtWii0oD6HfE03SzaJyUxxX_zbzbLr-gGBm8v95XBuDgAvMbrAGNH3KdVKLvDQt2h4BBa4a0lDOto_BguE6h31_XAGnpWyQQjhFtOn4IyQjjE6sAX4ees8lMHAuxwn6wJcaj1vZy8nFwOs_Qf7YH1MLtzDL9aaAq_rCaOfbdDWQLWD09rCqx8p21L2b-IIJVztpliidxre7XJM61jSWk6y2L3kMkvlTEzFlefgySh9sS-O9Rx8-3j1dfW5ubn9dL1a3jS6Gp0aqbCp1jklCPeKGGyI7NWoOB-54VwxihXqupZxayiVQx2xwVJmuUJEcdOeg8uDbprV1hptw5SlFym7rcw7EaUT_06CW4v7-CDatuccsSrw7iiQ4_fZlklsXdHWexlsnIsg-8-lhPW0om_-QzdxzqGuJzAilJKuJ6RSzYHSOZaS7Xgyg5HYJytSqpWIQ7KVf_33Bif6d5QVeHsEZNHSj1kG7cofjmFKe4Iq9-rAbcoU82lOcUeHoe3aX-lxtwM</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Meyer, Knut</creator><creator>Stecca, Kevin L.</creator><creator>Ewell-Hicks, Kim</creator><creator>Allen, Stephen M.</creator><creator>Everard, John D.</creator><general>American Society of Plant Biologists</general><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>3V.</scope><scope>4T-</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>S0X</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20120701</creationdate><title>Oil and Protein Accumulation in Developing Seeds Is Influenced by the Expression of a Cytosolic Pyrophosphatase in Arabidopsis</title><author>Meyer, Knut ; Stecca, Kevin L. ; Ewell-Hicks, Kim ; Allen, Stephen M. ; Everard, John D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c566t-ab1d131742018b2d1d2a8bfb77f7d77b641b055367ed44a9bfb69e46e7b02b7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>adenosine triphosphate</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>anaerobic conditions</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - growth & development</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>ATP</topic><topic>BIOCHEMICAL PROCESS AND MACROMOLECULAR STRUCTURES</topic><topic>Biochemical Processes and Macromolecular Structures</topic><topic>Biological and medical sciences</topic><topic>Biosynthesis</topic><topic>Biotechnology</topic><topic>carbon</topic><topic>Centrifugation, Density Gradient</topic><topic>Crosses, Genetic</topic><topic>cytosol</topic><topic>Cytosol - enzymology</topic><topic>Enzymes</topic><topic>filling period</topic><topic>fruits</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Plant</topic><topic>genes</topic><topic>Genes, Dominant - genetics</topic><topic>Genes, Plant - genetics</topic><topic>Genetic Association Studies</topic><topic>genetically modified organisms</topic><topic>Glycolysis</topic><topic>Hypoxia</topic><topic>Immunoblotting</topic><topic>lipid content</topic><topic>lipids</topic><topic>Models, Biological</topic><topic>Mutagenesis, Insertional - genetics</topic><topic>mutants</topic><topic>Mutation - genetics</topic><topic>Oils & fats</topic><topic>phenotype</topic><topic>Phenotypes</topic><topic>Phylogeny</topic><topic>Plant Oils - metabolism</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>Plants, Genetically Modified</topic><topic>Pyrophosphatases - genetics</topic><topic>Pyrophosphatases - metabolism</topic><topic>Reproducibility of Results</topic><topic>RNA</topic><topic>RNA Interference</topic><topic>Seed maturation</topic><topic>seed oils</topic><topic>Seed storage</topic><topic>Seeds</topic><topic>Seeds - growth & development</topic><topic>Seeds - metabolism</topic><topic>sequence analysis</topic><topic>starch</topic><topic>Starches</topic><topic>sucrose</topic><topic>Sugars</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meyer, Knut</creatorcontrib><creatorcontrib>Stecca, Kevin L.</creatorcontrib><creatorcontrib>Ewell-Hicks, Kim</creatorcontrib><creatorcontrib>Allen, Stephen M.</creatorcontrib><creatorcontrib>Everard, John D.</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</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>Meyer, Knut</au><au>Stecca, Kevin L.</au><au>Ewell-Hicks, Kim</au><au>Allen, Stephen M.</au><au>Everard, John D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oil and Protein Accumulation in Developing Seeds Is Influenced by the Expression of a Cytosolic Pyrophosphatase in Arabidopsis</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2012-07-01</date><risdate>2012</risdate><volume>159</volume><issue>3</issue><spage>1221</spage><epage>1234</epage><pages>1221-1234</pages><issn>0032-0889</issn><issn>1532-2548</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>This study describes a dominant low-seed-oil mutant (lo15571) of Arabidopsis (Arabidopsis thaliana) generated by enhancer tagging. Compositional analysis of developing siliques and mature seeds indicated reduced conversion of photoassimilates to oil. Immunoblot analysis revealed increased levels of At1g01050 protein in developing siliques of lo15571. At1g01050 encodes a soluble, cytosolic pyrophosphatase and is one of five closely related genes that share predicted cytosolic localization and at least 70% amino acid sequence identity. Expression of At1g01050 using a seed-preferred promoter recreated most features of the lo15571 seed phenotype, including low seed oil content and increased levels of transient starch and soluble sugars in developing siliques. Seed-preferred RNA interference-mediated silencing of Atlg01050 and At3g53620, a second cytosolic pyrophosphatase gene that shows expression during seed filling, led to a heritable oil increase of 1% to 4%, mostly at the expense of seed storage protein. These results are consistent with a scenario in which the rate of mobilization of sucrose, for precursor supply of seed storage lipid biosynthesis by cytosolic glycolysis, is strongly influenced by the expression of endogenous pyrophosphatase enzymes. This emphasizes the central role of pyrophosphate-dependent reactions supporting cytosolic glycolysis during seed maturation when ATP supply is low, presumably due to hypoxic conditions. This route is the major route providing precursors for seed oil biosynthesis. ATP-dependent reactions at the entry point of glycolysis in the cytosol or plastid cannot fully compensate for the loss of oil content observed in transgenic events with increased expression of cytosolic pyrophosphatase enzyme in the cytosol. These findings shed new light on the dynamic properties of cytosolic pyrophosphate pools in developing seed and their influence on carbon partitioning during seed filling. Finally, our work uniquely demonstrates that genes encoding cytosolic pyrophosphatase enzymes provide novel targets to improve seed composition for plant biotechnology applications.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>22566496</pmid><doi>10.1104/pp.112.198309</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 2012-07, Vol.159 (3), p.1221-1234 |
| issn | 0032-0889 1532-2548 1532-2548 |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | adenosine triphosphate amino acid sequences Amino acids anaerobic conditions Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - growth & development Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana ATP BIOCHEMICAL PROCESS AND MACROMOLECULAR STRUCTURES Biochemical Processes and Macromolecular Structures Biological and medical sciences Biosynthesis Biotechnology carbon Centrifugation, Density Gradient Crosses, Genetic cytosol Cytosol - enzymology Enzymes filling period fruits Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Plant genes Genes, Dominant - genetics Genes, Plant - genetics Genetic Association Studies genetically modified organisms Glycolysis Hypoxia Immunoblotting lipid content lipids Models, Biological Mutagenesis, Insertional - genetics mutants Mutation - genetics Oils & fats phenotype Phenotypes Phylogeny Plant Oils - metabolism Plant physiology and development Plants Plants, Genetically Modified Pyrophosphatases - genetics Pyrophosphatases - metabolism Reproducibility of Results RNA RNA Interference Seed maturation seed oils Seed storage Seeds Seeds - growth & development Seeds - metabolism sequence analysis starch Starches sucrose Sugars |
| title | Oil and Protein Accumulation in Developing Seeds Is Influenced by the Expression of a Cytosolic Pyrophosphatase in Arabidopsis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-12T11%3A20%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Oil%20and%20Protein%20Accumulation%20in%20Developing%20Seeds%20Is%20Influenced%20by%20the%20Expression%20of%20a%20Cytosolic%20Pyrophosphatase%20in%20Arabidopsis&rft.jtitle=Plant%20physiology%20(Bethesda)&rft.au=Meyer,%20Knut&rft.date=2012-07-01&rft.volume=159&rft.issue=3&rft.spage=1221&rft.epage=1234&rft.pages=1221-1234&rft.issn=0032-0889&rft.eissn=1532-2548&rft.coden=PPHYA5&rft_id=info:doi/10.1104/pp.112.198309&rft_dat=%3Cjstor_pubme%3E41549935%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1024425822&rft_id=info:pmid/22566496&rft_jstor_id=41549935&rfr_iscdi=true |