Subcellular pyrophosphate metabolism in developing tubers of potato (Solanum tuberosum)
PPi has previously been implicated specifically in the co-ordination of the sucrose-starch transition and in the broader context of its role as co-factor in heterotrophic plant metabolism. In order to assess the compartmentation of pyrophosphate (PPi) metabolism in the potato tuber we analysed the e...
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description | PPi has previously been implicated specifically in the co-ordination of the sucrose-starch transition and in the broader context of its role as co-factor in heterotrophic plant metabolism. In order to assess the compartmentation of pyrophosphate (PPi) metabolism in the potato tuber we analysed the effect of expressing a bacterial pyrophosphatase in the amyloplast of wild type tubers or in the cytosol or amyloplast of invertase-expressing tubers. The second and third approaches were adopted since we have previously characterized the invertase expressing lines to both exhibit highly altered sucrose metabolism and to contain elevated levels of PPi (Farré et al. (2000a) Plant Physiol 123:681) and therefore this background rendered questions concerning the level of communication between the plastidic and cytosolic pyrophosphate pools relatively facile. In this study we observed that the increase in PPi in the invertase expressing lines was mainly confined to the cytosol. Accordingly, the expression of a bacterial pyrophosphatase in the plastid of either wild type or invertase-expressing tubers did not lead to a decrease in total PPi content. However, the expression of the heterologous pyrophosphatase in the cytosol of cytosolic invertase-expressing tubers led to strong metabolic changes. These results are discussed both with respect to our previous hypotheses and to current models of the compartmentation of potato tuber metabolism. |
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In order to assess the compartmentation of pyrophosphate (PPi) metabolism in the potato tuber we analysed the effect of expressing a bacterial pyrophosphatase in the amyloplast of wild type tubers or in the cytosol or amyloplast of invertase-expressing tubers. The second and third approaches were adopted since we have previously characterized the invertase expressing lines to both exhibit highly altered sucrose metabolism and to contain elevated levels of PPi (Farré et al. (2000a) Plant Physiol 123:681) and therefore this background rendered questions concerning the level of communication between the plastidic and cytosolic pyrophosphate pools relatively facile. In this study we observed that the increase in PPi in the invertase expressing lines was mainly confined to the cytosol. Accordingly, the expression of a bacterial pyrophosphatase in the plastid of either wild type or invertase-expressing tubers did not lead to a decrease in total PPi content. However, the expression of the heterologous pyrophosphatase in the cytosol of cytosolic invertase-expressing tubers led to strong metabolic changes. These results are discussed both with respect to our previous hypotheses and to current models of the compartmentation of potato tuber metabolism.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1007/s11103-006-9011-4</identifier><identifier>PMID: 16915524</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>amyloplasts ; Bacterial Proteins - metabolism ; beta-fructofuranosidase ; carbohydrate metabolism ; cytosol ; Diphosphates - metabolism ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Metabolism ; Ordination ; Plant metabolism ; Plants, Genetically Modified - metabolism ; Potatoes ; pyrophosphatases ; Pyrophosphatases - genetics ; Pyrophosphatases - metabolism ; pyrophosphates ; Solanum tuberosum ; Solanum tuberosum - growth & development ; Solanum tuberosum - metabolism ; starch ; Starch - metabolism ; Subcellular Fractions - metabolism ; sucrose ; Sucrose - metabolism ; tubers</subject><ispartof>Plant molecular biology, 2006-09, Vol.62 (1-2), p.165-179</ispartof><rights>Springer Science+Business Media B.V. 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-cca417129279d9fed17564d16d368e69f14ba4276738098bb98765519cc24d2f3</citedby><cites>FETCH-LOGICAL-c381t-cca417129279d9fed17564d16d368e69f14ba4276738098bb98765519cc24d2f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16915524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Farre, E.M</creatorcontrib><creatorcontrib>Tech, S</creatorcontrib><creatorcontrib>Trethewey, R.N</creatorcontrib><creatorcontrib>Fernie, A.R</creatorcontrib><creatorcontrib>Willmitzer, L</creatorcontrib><title>Subcellular pyrophosphate metabolism in developing tubers of potato (Solanum tuberosum)</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>PPi has previously been implicated specifically in the co-ordination of the sucrose-starch transition and in the broader context of its role as co-factor in heterotrophic plant metabolism. In order to assess the compartmentation of pyrophosphate (PPi) metabolism in the potato tuber we analysed the effect of expressing a bacterial pyrophosphatase in the amyloplast of wild type tubers or in the cytosol or amyloplast of invertase-expressing tubers. The second and third approaches were adopted since we have previously characterized the invertase expressing lines to both exhibit highly altered sucrose metabolism and to contain elevated levels of PPi (Farré et al. (2000a) Plant Physiol 123:681) and therefore this background rendered questions concerning the level of communication between the plastidic and cytosolic pyrophosphate pools relatively facile. In this study we observed that the increase in PPi in the invertase expressing lines was mainly confined to the cytosol. Accordingly, the expression of a bacterial pyrophosphatase in the plastid of either wild type or invertase-expressing tubers did not lead to a decrease in total PPi content. However, the expression of the heterologous pyrophosphatase in the cytosol of cytosolic invertase-expressing tubers led to strong metabolic changes. These results are discussed both with respect to our previous hypotheses and to current models of the compartmentation of potato tuber metabolism.</description><subject>amyloplasts</subject><subject>Bacterial Proteins - metabolism</subject><subject>beta-fructofuranosidase</subject><subject>carbohydrate metabolism</subject><subject>cytosol</subject><subject>Diphosphates - metabolism</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Metabolism</subject><subject>Ordination</subject><subject>Plant metabolism</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Potatoes</subject><subject>pyrophosphatases</subject><subject>Pyrophosphatases - genetics</subject><subject>Pyrophosphatases - metabolism</subject><subject>pyrophosphates</subject><subject>Solanum tuberosum</subject><subject>Solanum tuberosum - growth & development</subject><subject>Solanum tuberosum - metabolism</subject><subject>starch</subject><subject>Starch - metabolism</subject><subject>Subcellular Fractions - metabolism</subject><subject>sucrose</subject><subject>Sucrose - metabolism</subject><subject>tubers</subject><issn>0167-4412</issn><issn>1573-5028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</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>eNqFkctKxTAURYMoen18gBMtDkQH1ZwkzWMo4gsEB1dxGNI21Urb1KQR_Htz6QXBiaMMztobdhZCh4AvAGNxGQAA0xxjnisMkLMNtIBC0LzARG6iBQYucsaA7KDdED4wTinKt9EOcAVFQdgCvS5jWdmui53x2fjt3fjuwvhuJpv1djKl69rQZ-2Q1fbLdm5sh7dsiqX1IXNNNrrJTC47W7rODLGfLy7E_nwfbTWmC_Zg_e6hl9ub5-v7_PHp7uH66jGvqIQpryrDQABRRKhaNbYGUXBWA68pl5arBlhpGBFcUImVLEslBS8KUFVFWE0auodO597Ru89ow6T7NqwGmcG6GDSXkipg5F-QpHoiiUrgyR_ww0U_pBFarL6NCUkTBDNUpbnB20aPvu2N_9aA9cqNnt3o5Eav3GiWMkfr4lj2tv5NrGUk4HgGGuO0efNt0C9LgoGmfBKaxP4A_sSSPQ</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Farre, E.M</creator><creator>Tech, S</creator><creator>Trethewey, R.N</creator><creator>Fernie, A.R</creator><creator>Willmitzer, L</creator><general>Springer Nature B.V</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>3V.</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20060901</creationdate><title>Subcellular pyrophosphate metabolism in developing tubers of potato (Solanum tuberosum)</title><author>Farre, E.M ; Tech, S ; Trethewey, R.N ; Fernie, A.R ; Willmitzer, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-cca417129279d9fed17564d16d368e69f14ba4276738098bb98765519cc24d2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>amyloplasts</topic><topic>Bacterial Proteins - metabolism</topic><topic>beta-fructofuranosidase</topic><topic>carbohydrate metabolism</topic><topic>cytosol</topic><topic>Diphosphates - metabolism</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Metabolism</topic><topic>Ordination</topic><topic>Plant metabolism</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Potatoes</topic><topic>pyrophosphatases</topic><topic>Pyrophosphatases - genetics</topic><topic>Pyrophosphatases - metabolism</topic><topic>pyrophosphates</topic><topic>Solanum tuberosum</topic><topic>Solanum tuberosum - growth & development</topic><topic>Solanum tuberosum - metabolism</topic><topic>starch</topic><topic>Starch - metabolism</topic><topic>Subcellular Fractions - metabolism</topic><topic>sucrose</topic><topic>Sucrose - metabolism</topic><topic>tubers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Farre, E.M</creatorcontrib><creatorcontrib>Tech, S</creatorcontrib><creatorcontrib>Trethewey, R.N</creatorcontrib><creatorcontrib>Fernie, A.R</creatorcontrib><creatorcontrib>Willmitzer, L</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>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</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>ProQuest Pharma Collection</collection><collection>Technology Research Database</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>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>Engineering Research Database</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>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</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>Genetics Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Plant molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Farre, E.M</au><au>Tech, S</au><au>Trethewey, R.N</au><au>Fernie, A.R</au><au>Willmitzer, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subcellular pyrophosphate metabolism in developing tubers of potato (Solanum tuberosum)</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>62</volume><issue>1-2</issue><spage>165</spage><epage>179</epage><pages>165-179</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><abstract>PPi has previously been implicated specifically in the co-ordination of the sucrose-starch transition and in the broader context of its role as co-factor in heterotrophic plant metabolism. In order to assess the compartmentation of pyrophosphate (PPi) metabolism in the potato tuber we analysed the effect of expressing a bacterial pyrophosphatase in the amyloplast of wild type tubers or in the cytosol or amyloplast of invertase-expressing tubers. The second and third approaches were adopted since we have previously characterized the invertase expressing lines to both exhibit highly altered sucrose metabolism and to contain elevated levels of PPi (Farré et al. (2000a) Plant Physiol 123:681) and therefore this background rendered questions concerning the level of communication between the plastidic and cytosolic pyrophosphate pools relatively facile. In this study we observed that the increase in PPi in the invertase expressing lines was mainly confined to the cytosol. Accordingly, the expression of a bacterial pyrophosphatase in the plastid of either wild type or invertase-expressing tubers did not lead to a decrease in total PPi content. However, the expression of the heterologous pyrophosphatase in the cytosol of cytosolic invertase-expressing tubers led to strong metabolic changes. These results are discussed both with respect to our previous hypotheses and to current models of the compartmentation of potato tuber metabolism.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>16915524</pmid><doi>10.1007/s11103-006-9011-4</doi><tpages>15</tpages></addata></record> |
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subjects | amyloplasts Bacterial Proteins - metabolism beta-fructofuranosidase carbohydrate metabolism cytosol Diphosphates - metabolism Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Metabolism Ordination Plant metabolism Plants, Genetically Modified - metabolism Potatoes pyrophosphatases Pyrophosphatases - genetics Pyrophosphatases - metabolism pyrophosphates Solanum tuberosum Solanum tuberosum - growth & development Solanum tuberosum - metabolism starch Starch - metabolism Subcellular Fractions - metabolism sucrose Sucrose - metabolism tubers |
title | Subcellular pyrophosphate metabolism in developing tubers of potato (Solanum tuberosum) |
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