PHA production, from bacteria to plants
The genes encoding the polyhydroxyalkanoate (PHA) biosynthetic pathway in Ralstonia eutropha (3-ketothiolase, phaA or bktB; acetoacetyl-CoA reductase, phaB; and PHA synthase, phaC) were engineered for plant plastid targeting and expressed using leaf (e35S) or seed-specific (7s or lesquerella hydroxy...
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Veröffentlicht in: | International journal of biological macromolecules 1999-06, Vol.25 (1), p.303-306 |
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creator | Valentin, Henry E. Broyles, Debra L. Casagrande, Laura A. Colburn, Susan M. Creely, Wendi L. DeLaquil, Pamela A. Felton, Heather M. Gonzalez, Kathleen A. Houmiel, Kathryn L. Lutke, Kevin Mahadeo, Debbie A. Mitsky, Timothy A. Padgette, Stephen R. Reiser, Steven E. Slater, Steven Stark, David M. Stock, Robert T. Stone, Deborah A. Taylor, Nancy B. Thorne, Gregory M. Tran, Minhtien Gruys, Kenneth J. |
description | The genes encoding the polyhydroxyalkanoate (PHA) biosynthetic pathway in
Ralstonia eutropha (3-ketothiolase,
phaA or
bktB; acetoacetyl-CoA reductase,
phaB; and PHA synthase,
phaC) were engineered for plant plastid targeting and expressed using leaf (e35S) or seed-specific (7s or
lesquerella hydroxylase) promoters in
Arabidopsis and
Brassica. PHA yields in homozygous transformants were 12–13% of the dry mass in homozygous
Arabidopsis plants and approximately 7% of the seed weight in seeds from heterozygous canola plants. When a threonine deaminase was expressed in addition to
bktB,
phaB and
phaC, a copolyester of 3-hydroxybutyrate and 3-hydroxyvalerate was produced in both
Arabidopsis and
Brassica. |
doi_str_mv | 10.1016/S0141-8130(99)00045-8 |
format | Article |
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Ralstonia eutropha (3-ketothiolase,
phaA or
bktB; acetoacetyl-CoA reductase,
phaB; and PHA synthase,
phaC) were engineered for plant plastid targeting and expressed using leaf (e35S) or seed-specific (7s or
lesquerella hydroxylase) promoters in
Arabidopsis and
Brassica. PHA yields in homozygous transformants were 12–13% of the dry mass in homozygous
Arabidopsis plants and approximately 7% of the seed weight in seeds from heterozygous canola plants. When a threonine deaminase was expressed in addition to
bktB,
phaB and
phaC, a copolyester of 3-hydroxybutyrate and 3-hydroxyvalerate was produced in both
Arabidopsis and
Brassica.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/S0141-8130(99)00045-8</identifier><identifier>PMID: 10416678</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Acetyl-CoA C-Acyltransferase - genetics ; Acetyl-CoA C-Acyltransferase - metabolism ; Acyltransferases - genetics ; Acyltransferases - metabolism ; Alcohol Oxidoreductases - genetics ; Alcohol Oxidoreductases - metabolism ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Cupriavidus necator - enzymology ; Cupriavidus necator - genetics ; Homozygote ; Models, Molecular ; Molecular Structure ; Plant Leaves ; Plants - metabolism ; Plants, Genetically Modified ; Polyesters - metabolism ; Recombinant Proteins - metabolism ; Seeds</subject><ispartof>International journal of biological macromolecules, 1999-06, Vol.25 (1), p.303-306</ispartof><rights>1999 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c361t-7d12667bec7d327db77c49a3b9ae5939bd329a90974e4191f640fc45a5ddb3ae3</citedby><cites>FETCH-LOGICAL-c361t-7d12667bec7d327db77c49a3b9ae5939bd329a90974e4191f640fc45a5ddb3ae3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0141-8130(99)00045-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3554,27933,27934,46004</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10416678$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Valentin, Henry E.</creatorcontrib><creatorcontrib>Broyles, Debra L.</creatorcontrib><creatorcontrib>Casagrande, Laura A.</creatorcontrib><creatorcontrib>Colburn, Susan M.</creatorcontrib><creatorcontrib>Creely, Wendi L.</creatorcontrib><creatorcontrib>DeLaquil, Pamela A.</creatorcontrib><creatorcontrib>Felton, Heather M.</creatorcontrib><creatorcontrib>Gonzalez, Kathleen A.</creatorcontrib><creatorcontrib>Houmiel, Kathryn L.</creatorcontrib><creatorcontrib>Lutke, Kevin</creatorcontrib><creatorcontrib>Mahadeo, Debbie A.</creatorcontrib><creatorcontrib>Mitsky, Timothy A.</creatorcontrib><creatorcontrib>Padgette, Stephen R.</creatorcontrib><creatorcontrib>Reiser, Steven E.</creatorcontrib><creatorcontrib>Slater, Steven</creatorcontrib><creatorcontrib>Stark, David M.</creatorcontrib><creatorcontrib>Stock, Robert T.</creatorcontrib><creatorcontrib>Stone, Deborah A.</creatorcontrib><creatorcontrib>Taylor, Nancy B.</creatorcontrib><creatorcontrib>Thorne, Gregory M.</creatorcontrib><creatorcontrib>Tran, Minhtien</creatorcontrib><creatorcontrib>Gruys, Kenneth J.</creatorcontrib><title>PHA production, from bacteria to plants</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>The genes encoding the polyhydroxyalkanoate (PHA) biosynthetic pathway in
Ralstonia eutropha (3-ketothiolase,
phaA or
bktB; acetoacetyl-CoA reductase,
phaB; and PHA synthase,
phaC) were engineered for plant plastid targeting and expressed using leaf (e35S) or seed-specific (7s or
lesquerella hydroxylase) promoters in
Arabidopsis and
Brassica. PHA yields in homozygous transformants were 12–13% of the dry mass in homozygous
Arabidopsis plants and approximately 7% of the seed weight in seeds from heterozygous canola plants. When a threonine deaminase was expressed in addition to
bktB,
phaB and
phaC, a copolyester of 3-hydroxybutyrate and 3-hydroxyvalerate was produced in both
Arabidopsis and
Brassica.</description><subject>Acetyl-CoA C-Acyltransferase - genetics</subject><subject>Acetyl-CoA C-Acyltransferase - metabolism</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Alcohol Oxidoreductases - genetics</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Cupriavidus necator - enzymology</subject><subject>Cupriavidus necator - genetics</subject><subject>Homozygote</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Plant Leaves</subject><subject>Plants - metabolism</subject><subject>Plants, Genetically Modified</subject><subject>Polyesters - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Seeds</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUF1LwzAUDaK4Of0JSp_8AKvJkja9TzKGOmGgoD6HNLmFSLvOpBX892brEN98utzDueecewg5ZfSGUZbfvlImWFowTi8BriilIkuLPTJmhYQ0rnyfjH8pI3IUwkdE84wVh2TEqGB5LosxuXhZzJK1b21vOteurpPKt01SatOhdzrp2mRd61UXjslBpeuAJ7s5Ie8P92_zRbp8fnyaz5ap4TnrUmnZNAqXaKTlU2lLKY0AzUvQmAGHMqKggYIUKBiwKhe0MiLTmbUl18gn5HzQjZk-ewydalwwWMcQ2PZB5VAAiCg1IdlANL4NwWOl1t412n8rRtWmIbVtSG3eVwBq25Aq4t3ZzqAvG7R_roZKIuFuIGB888uhV8E4XBm0zqPplG3dPxY_JyRzxA</recordid><startdate>19990601</startdate><enddate>19990601</enddate><creator>Valentin, Henry E.</creator><creator>Broyles, Debra L.</creator><creator>Casagrande, Laura A.</creator><creator>Colburn, Susan M.</creator><creator>Creely, Wendi L.</creator><creator>DeLaquil, Pamela A.</creator><creator>Felton, Heather M.</creator><creator>Gonzalez, Kathleen A.</creator><creator>Houmiel, Kathryn L.</creator><creator>Lutke, Kevin</creator><creator>Mahadeo, Debbie A.</creator><creator>Mitsky, Timothy A.</creator><creator>Padgette, Stephen R.</creator><creator>Reiser, Steven E.</creator><creator>Slater, Steven</creator><creator>Stark, David M.</creator><creator>Stock, Robert T.</creator><creator>Stone, Deborah A.</creator><creator>Taylor, Nancy B.</creator><creator>Thorne, Gregory M.</creator><creator>Tran, Minhtien</creator><creator>Gruys, Kenneth J.</creator><general>Elsevier B.V</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></search><sort><creationdate>19990601</creationdate><title>PHA production, from bacteria to plants</title><author>Valentin, Henry E. ; Broyles, Debra L. ; Casagrande, Laura A. ; Colburn, Susan M. ; Creely, Wendi L. ; DeLaquil, Pamela A. ; Felton, Heather M. ; Gonzalez, Kathleen A. ; Houmiel, Kathryn L. ; Lutke, Kevin ; Mahadeo, Debbie A. ; Mitsky, Timothy A. ; Padgette, Stephen R. ; Reiser, Steven E. ; Slater, Steven ; Stark, David M. ; Stock, Robert T. ; Stone, Deborah A. ; Taylor, Nancy B. ; Thorne, Gregory M. ; Tran, Minhtien ; Gruys, Kenneth J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c361t-7d12667bec7d327db77c49a3b9ae5939bd329a90974e4191f640fc45a5ddb3ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Acetyl-CoA C-Acyltransferase - genetics</topic><topic>Acetyl-CoA C-Acyltransferase - metabolism</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Alcohol Oxidoreductases - genetics</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Cupriavidus necator - enzymology</topic><topic>Cupriavidus necator - genetics</topic><topic>Homozygote</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Plant Leaves</topic><topic>Plants - metabolism</topic><topic>Plants, Genetically Modified</topic><topic>Polyesters - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Seeds</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Valentin, Henry E.</creatorcontrib><creatorcontrib>Broyles, Debra L.</creatorcontrib><creatorcontrib>Casagrande, Laura A.</creatorcontrib><creatorcontrib>Colburn, Susan M.</creatorcontrib><creatorcontrib>Creely, Wendi L.</creatorcontrib><creatorcontrib>DeLaquil, Pamela A.</creatorcontrib><creatorcontrib>Felton, Heather M.</creatorcontrib><creatorcontrib>Gonzalez, Kathleen A.</creatorcontrib><creatorcontrib>Houmiel, Kathryn L.</creatorcontrib><creatorcontrib>Lutke, Kevin</creatorcontrib><creatorcontrib>Mahadeo, Debbie A.</creatorcontrib><creatorcontrib>Mitsky, Timothy A.</creatorcontrib><creatorcontrib>Padgette, Stephen R.</creatorcontrib><creatorcontrib>Reiser, Steven E.</creatorcontrib><creatorcontrib>Slater, Steven</creatorcontrib><creatorcontrib>Stark, David M.</creatorcontrib><creatorcontrib>Stock, Robert T.</creatorcontrib><creatorcontrib>Stone, Deborah A.</creatorcontrib><creatorcontrib>Taylor, Nancy B.</creatorcontrib><creatorcontrib>Thorne, Gregory M.</creatorcontrib><creatorcontrib>Tran, Minhtien</creatorcontrib><creatorcontrib>Gruys, Kenneth J.</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><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Valentin, Henry E.</au><au>Broyles, Debra L.</au><au>Casagrande, Laura A.</au><au>Colburn, Susan M.</au><au>Creely, Wendi L.</au><au>DeLaquil, Pamela A.</au><au>Felton, Heather M.</au><au>Gonzalez, Kathleen A.</au><au>Houmiel, Kathryn L.</au><au>Lutke, Kevin</au><au>Mahadeo, Debbie A.</au><au>Mitsky, Timothy A.</au><au>Padgette, Stephen R.</au><au>Reiser, Steven E.</au><au>Slater, Steven</au><au>Stark, David M.</au><au>Stock, Robert T.</au><au>Stone, Deborah A.</au><au>Taylor, Nancy B.</au><au>Thorne, Gregory M.</au><au>Tran, Minhtien</au><au>Gruys, Kenneth J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PHA production, from bacteria to plants</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>1999-06-01</date><risdate>1999</risdate><volume>25</volume><issue>1</issue><spage>303</spage><epage>306</epage><pages>303-306</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>The genes encoding the polyhydroxyalkanoate (PHA) biosynthetic pathway in
Ralstonia eutropha (3-ketothiolase,
phaA or
bktB; acetoacetyl-CoA reductase,
phaB; and PHA synthase,
phaC) were engineered for plant plastid targeting and expressed using leaf (e35S) or seed-specific (7s or
lesquerella hydroxylase) promoters in
Arabidopsis and
Brassica. PHA yields in homozygous transformants were 12–13% of the dry mass in homozygous
Arabidopsis plants and approximately 7% of the seed weight in seeds from heterozygous canola plants. When a threonine deaminase was expressed in addition to
bktB,
phaB and
phaC, a copolyester of 3-hydroxybutyrate and 3-hydroxyvalerate was produced in both
Arabidopsis and
Brassica.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>10416678</pmid><doi>10.1016/S0141-8130(99)00045-8</doi><tpages>4</tpages></addata></record> |
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language | eng |
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source | MEDLINE; Access via ScienceDirect (Elsevier) |
subjects | Acetyl-CoA C-Acyltransferase - genetics Acetyl-CoA C-Acyltransferase - metabolism Acyltransferases - genetics Acyltransferases - metabolism Alcohol Oxidoreductases - genetics Alcohol Oxidoreductases - metabolism Arabidopsis - genetics Arabidopsis - metabolism Cupriavidus necator - enzymology Cupriavidus necator - genetics Homozygote Models, Molecular Molecular Structure Plant Leaves Plants - metabolism Plants, Genetically Modified Polyesters - metabolism Recombinant Proteins - metabolism Seeds |
title | PHA production, from bacteria to plants |
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