Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene
Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is ba...
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| Veröffentlicht in: | Transgenic research 2000-04, Vol.9 (2), p.137-144 |
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| creator | GALILI, S GUENOUNE, D WININGER, S HANA, B SCHUPPER, A BEN-DOR, B KAPULNIK, Y |
| description | Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins. |
| doi_str_mv | 10.1023/A:1008991625001 |
| format | Article |
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Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins.</description><identifier>ISSN: 0962-8819</identifier><identifier>EISSN: 1573-9368</identifier><identifier>DOI: 10.1023/A:1008991625001</identifier><identifier>PMID: 10951697</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Amino acids ; Aspartate Kinase - genetics ; Aspartate Kinase - metabolism ; Biological and medical sciences ; Biotechnology ; E coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genetic engineering ; Genetic technics ; Medicago sativa ; Medicago sativa - genetics ; Medicago sativa - metabolism ; Methods. Procedures. Technologies ; Plant Leaves - metabolism ; Plants, Genetically Modified - metabolism ; Protein Binding ; Recombinant Proteins - metabolism ; threonine ; Threonine - biosynthesis ; Transgenic animals and transgenic plants ; Transgenic plants</subject><ispartof>Transgenic research, 2000-04, Vol.9 (2), p.137-144</ispartof><rights>2000 INIST-CNRS</rights><rights>Kluwer Academic Publishers 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-1466a5685e49c96ef4f9e5126b453cc5aee7d93e6c91e87d9699bed9f08bec923</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1448376$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10951697$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GALILI, S</creatorcontrib><creatorcontrib>GUENOUNE, D</creatorcontrib><creatorcontrib>WININGER, S</creatorcontrib><creatorcontrib>HANA, B</creatorcontrib><creatorcontrib>SCHUPPER, A</creatorcontrib><creatorcontrib>BEN-DOR, B</creatorcontrib><creatorcontrib>KAPULNIK, Y</creatorcontrib><title>Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene</title><title>Transgenic research</title><addtitle>Transgenic Res</addtitle><description>Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins.</description><subject>Amino acids</subject><subject>Aspartate Kinase - genetics</subject><subject>Aspartate Kinase - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>E coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Medicago sativa</subject><subject>Medicago sativa - genetics</subject><subject>Medicago sativa - metabolism</subject><subject>Methods. Procedures. Technologies</subject><subject>Plant Leaves - metabolism</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - metabolism</subject><subject>threonine</subject><subject>Threonine - biosynthesis</subject><subject>Transgenic animals and transgenic plants</subject><subject>Transgenic plants</subject><issn>0962-8819</issn><issn>1573-9368</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqF0UFrFTEQB_Agin22nr1JECn2sDXZbLKZ3kqprfDESz0vs9nZ17T7ss8kW_Tb9KMa8YnQixBIBn78w8ww9kaKUylq9fH8TAphAaSptRDyGVtJ3aoKlLHP2UqAqStrJRywVyndFVCweskOpAAtDbQr9ngZbjE4GvhEDzQlPo98jEQcw8B3cc7kQ9XPS6nybaQ5-EDcB54jhrSh4B3Hafx9-IcvNHiHm5knzP4B-fr0hNOPXaSUfNhw5D26TNHjxEeioVT3lQ-JQvLFly_TDmPGTPzeB0zESz4dsRclPtHr_X3Ivn26vLm4rtZfrz5fnK8rpxqRK9kYg9pYTQ04MDQ2I5CWtekbrZzTSNQOoMg4kGTL0wD0NMAobE8OanXIjv_klqa_L5Ryt_XJ0TRhoHlJXStbrQWo_0LZGl0LKwp89wTezUsMpYmu1UoDNEoW9HaPln5LQ7eLfovxZ_d3QwW83wNMrsy5zN359M81jVWtUb8AKxKhVw</recordid><startdate>20000401</startdate><enddate>20000401</enddate><creator>GALILI, S</creator><creator>GUENOUNE, D</creator><creator>WININGER, S</creator><creator>HANA, B</creator><creator>SCHUPPER, A</creator><creator>BEN-DOR, B</creator><creator>KAPULNIK, Y</creator><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7TK</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>ABUWG</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>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7QO</scope><scope>7X8</scope></search><sort><creationdate>20000401</creationdate><title>Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene</title><author>GALILI, S ; GUENOUNE, D ; WININGER, S ; HANA, B ; SCHUPPER, A ; BEN-DOR, B ; KAPULNIK, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-1466a5685e49c96ef4f9e5126b453cc5aee7d93e6c91e87d9699bed9f08bec923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino acids</topic><topic>Aspartate Kinase - genetics</topic><topic>Aspartate Kinase - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>E coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Medicago sativa</topic><topic>Medicago sativa - genetics</topic><topic>Medicago sativa - metabolism</topic><topic>Methods. Procedures. Technologies</topic><topic>Plant Leaves - metabolism</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - metabolism</topic><topic>threonine</topic><topic>Threonine - biosynthesis</topic><topic>Transgenic animals and transgenic plants</topic><topic>Transgenic plants</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GALILI, S</creatorcontrib><creatorcontrib>GUENOUNE, D</creatorcontrib><creatorcontrib>WININGER, S</creatorcontrib><creatorcontrib>HANA, B</creatorcontrib><creatorcontrib>SCHUPPER, A</creatorcontrib><creatorcontrib>BEN-DOR, B</creatorcontrib><creatorcontrib>KAPULNIK, Y</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>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</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>ProQuest Central (Alumni Edition)</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>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>Biological Science Database</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 China</collection><collection>Genetics Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Transgenic research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GALILI, S</au><au>GUENOUNE, D</au><au>WININGER, S</au><au>HANA, B</au><au>SCHUPPER, A</au><au>BEN-DOR, B</au><au>KAPULNIK, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene</atitle><jtitle>Transgenic research</jtitle><addtitle>Transgenic Res</addtitle><date>2000-04-01</date><risdate>2000</risdate><volume>9</volume><issue>2</issue><spage>137</spage><epage>144</epage><pages>137-144</pages><issn>0962-8819</issn><eissn>1573-9368</eissn><abstract>Threonine, lysine, methionine, and tryptophan are essential amino acids for humans and monogastric animals. Many of the commonly used diet formulations, particularly for pigs and poultry, contain limiting amounts of these amino acids. One approach for raising the level of essential amino acids is based on altering the regulation of their biosynthetic pathways in transgenic plants. Here we describe the first production of a transgenic forage plant, alfalfa (Medicago sativa L.) with modified regulation of the aspartate-family amino acid biosynthetic pathway. This was achieved by over-expressing the Escherichia coli feedback-insensitive aspartate kinase (AK) in transgenic plants. These plants showed enhanced levels of both free and protein-bound threonine. In many transgenic plants the rise in free threonine was accompanied by a significant reduction both in aspartate and in glutamate. Our data suggest that in alfalfa, AK might not be the only limiting factor for threonine biosynthesis, and that the free threonine pool in this plant limits its incorporation into plant proteins.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>10951697</pmid><doi>10.1023/A:1008991625001</doi><tpages>8</tpages></addata></record> |
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| ispartof | Transgenic research, 2000-04, Vol.9 (2), p.137-144 |
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| subjects | Amino acids Aspartate Kinase - genetics Aspartate Kinase - metabolism Biological and medical sciences Biotechnology E coli Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genetic engineering Genetic technics Medicago sativa Medicago sativa - genetics Medicago sativa - metabolism Methods. Procedures. Technologies Plant Leaves - metabolism Plants, Genetically Modified - metabolism Protein Binding Recombinant Proteins - metabolism threonine Threonine - biosynthesis Transgenic animals and transgenic plants Transgenic plants |
| title | Enhanced levels of free and protein-bound threonine in transgenic alfalfa (Medicago sativa L.) expressing a bacterial feedback-insensitive aspartate kinase gene |
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