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Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris
Lysine and threonine overproducer mutants in Nicotiana sylvestris, characterized by an altered regulation of, respectively, dihydrodipicolinate synthase and aspartate kinase activities, were crossed to assess the effects of the simultaneous presence of these genes on the biosynthesis of aspartate-de...
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| Published in: | Plant physiology (Bethesda) 1992-08, Vol.99 (4), p.1285-1293 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 1293 |
| container_issue | 4 |
| container_start_page | 1285 |
| container_title | Plant physiology (Bethesda) |
| container_volume | 99 |
| creator | Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium) Ghislain, M Jacobs, M |
| description | Lysine and threonine overproducer mutants in Nicotiana sylvestris, characterized by an altered regulation of, respectively, dihydrodipicolinate synthase and aspartate kinase activities, were crossed to assess the effects of the simultaneous presence of these genes on the biosynthesis of aspartate-derived amino acids. The monogenic dominant behavior of both resistance traits was confirmed, and their loci were found to be unlinked. Study of the inhibition properties of dihydrodipicolinate synthase and aspartate kinase activities in RAEC-1 X RLT 70 confirmed the heterozygote state of both mutations, because only half of their lysine-sensitive activity could still be inhibited by this negative effector. Analysis of the free amino acid pool during the growth of the double mutant revealed a major free lysine overproduction reaching up to 50% of the total pool, whereas the other aspartate-derived amino acids remained equally or even less abundant than in the wild type. An abnormal phenotype was clearly associated with such high levels of lysine accumulation, which points out the possible role of this amino acid in the developmental features of the plant. Comparison of the amino acid content, free and total (free + protein-bound), between the wild type, the two mutants, and the double mutant obtained by crossing them brings new insights on the regulation of the aspartate pathway, and on its implications in relationship to plant nutritional value improvement |
| doi_str_mv | 10.1104/pp.99.4.1285 |
| format | article |
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(Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium) ; Ghislain, M ; Jacobs, M</creator><creatorcontrib>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium) ; Ghislain, M ; Jacobs, M</creatorcontrib><description>Lysine and threonine overproducer mutants in Nicotiana sylvestris, characterized by an altered regulation of, respectively, dihydrodipicolinate synthase and aspartate kinase activities, were crossed to assess the effects of the simultaneous presence of these genes on the biosynthesis of aspartate-derived amino acids. The monogenic dominant behavior of both resistance traits was confirmed, and their loci were found to be unlinked. Study of the inhibition properties of dihydrodipicolinate synthase and aspartate kinase activities in RAEC-1 X RLT 70 confirmed the heterozygote state of both mutations, because only half of their lysine-sensitive activity could still be inhibited by this negative effector. Analysis of the free amino acid pool during the growth of the double mutant revealed a major free lysine overproduction reaching up to 50% of the total pool, whereas the other aspartate-derived amino acids remained equally or even less abundant than in the wild type. An abnormal phenotype was clearly associated with such high levels of lysine accumulation, which points out the possible role of this amino acid in the developmental features of the plant. Comparison of the amino acid content, free and total (free + protein-bound), between the wild type, the two mutants, and the double mutant obtained by crossing them brings new insights on the regulation of the aspartate pathway, and on its implications in relationship to plant nutritional value improvement</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.99.4.1285</identifier><identifier>PMID: 16669034</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>ACIDE AMINE ; ACIDE ASPARTIQUE ; ACIDO ASPARTICO ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Amino acids ; AMINOACIDOS ; Biological and medical sciences ; BIOSINTESIS ; BIOSYNTHESE ; Biosynthesis ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gene expression regulation ; GENETICA ; GENETIQUE ; Heterozygotes ; Leaves ; LIGASAS ; LIGASE ; Metabolism ; Metabolism and Enzymology ; MUTANT ; MUTANTES ; NICOTIANA ; Nitrogen metabolism ; Overproduction ; Percentages ; Phenotypes ; Plant physiology and development ; Plants ; TRANSFERASAS ; TRANSFERASE ; VIA BIOQUIMICA DEL METABOLISMO ; VOIE BIOCHIMIQUE DU METABOLISME</subject><ispartof>Plant physiology (Bethesda), 1992-08, Vol.99 (4), p.1285-1293</ispartof><rights>Copyright 1992 American Society of Plant Physiologists</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3465-8a5a9797dfaf9cef33733435e27393c71849add7df5a38337b7cc7e47a2930683</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4274506$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4274506$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,58238,58471</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4917184$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16669034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium)</creatorcontrib><creatorcontrib>Ghislain, M</creatorcontrib><creatorcontrib>Jacobs, M</creatorcontrib><title>Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Lysine and threonine overproducer mutants in Nicotiana sylvestris, characterized by an altered regulation of, respectively, dihydrodipicolinate synthase and aspartate kinase activities, were crossed to assess the effects of the simultaneous presence of these genes on the biosynthesis of aspartate-derived amino acids. The monogenic dominant behavior of both resistance traits was confirmed, and their loci were found to be unlinked. Study of the inhibition properties of dihydrodipicolinate synthase and aspartate kinase activities in RAEC-1 X RLT 70 confirmed the heterozygote state of both mutations, because only half of their lysine-sensitive activity could still be inhibited by this negative effector. Analysis of the free amino acid pool during the growth of the double mutant revealed a major free lysine overproduction reaching up to 50% of the total pool, whereas the other aspartate-derived amino acids remained equally or even less abundant than in the wild type. An abnormal phenotype was clearly associated with such high levels of lysine accumulation, which points out the possible role of this amino acid in the developmental features of the plant. Comparison of the amino acid content, free and total (free + protein-bound), between the wild type, the two mutants, and the double mutant obtained by crossing them brings new insights on the regulation of the aspartate pathway, and on its implications in relationship to plant nutritional value improvement</description><subject>ACIDE AMINE</subject><subject>ACIDE ASPARTIQUE</subject><subject>ACIDO ASPARTICO</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Amino acids</subject><subject>AMINOACIDOS</subject><subject>Biological and medical sciences</subject><subject>BIOSINTESIS</subject><subject>BIOSYNTHESE</subject><subject>Biosynthesis</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression regulation</subject><subject>GENETICA</subject><subject>GENETIQUE</subject><subject>Heterozygotes</subject><subject>Leaves</subject><subject>LIGASAS</subject><subject>LIGASE</subject><subject>Metabolism</subject><subject>Metabolism and Enzymology</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>NICOTIANA</subject><subject>Nitrogen metabolism</subject><subject>Overproduction</subject><subject>Percentages</subject><subject>Phenotypes</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>VIA BIOQUIMICA DEL METABOLISMO</subject><subject>VOIE BIOCHIMIQUE DU METABOLISME</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNpFkEFv1DAQRi0EotvCjRNCyIdKXMhix3YcH1HVUqQKhGjP1qwzpi7ZJHiyrZZfj5ddtacZ6T19M_oYeyPFUkqhP03T0rmlXsq6Nc_YQhpVV7XR7XO2EKLsom3dETsmuhNCSCX1S3Ykm6ZxQukF-3H9MPKI2K0g_K7SQDhQmtM9chz-btdIfIx8vkUONEGeYUY-wXz7AFueBv4thXFOMACnbX-PNOdEr9iLCD3h68M8YTcX59dnl9XV9y9fzz5fVUHpxlQtGHDW2S5CdAGjUlYprQzWVjkVrGy1g64r3IBqC13ZECxqC7VTomnVCfuwz53y-GdTbvt1ooB9DwOOG_K7OKftf_Pj3gx5JMoY_ZTTGvLWS-F3Hfpp8s557XcdFv39IXizWmP3JB9KK8LpQQAK0McMQ0j06Gknd98X7d1eu6N5zE-4ttqIpuC3exxh9PCrNOdvfjotTOOU-gfGDYsX</recordid><startdate>199208</startdate><enddate>199208</enddate><creator>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium)</creator><creator>Ghislain, M</creator><creator>Jacobs, M</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199208</creationdate><title>Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris</title><author>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium) ; Ghislain, M ; Jacobs, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3465-8a5a9797dfaf9cef33733435e27393c71849add7df5a38337b7cc7e47a2930683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ACIDE AMINE</topic><topic>ACIDE ASPARTIQUE</topic><topic>ACIDO ASPARTICO</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Amino acids</topic><topic>AMINOACIDOS</topic><topic>Biological and medical sciences</topic><topic>BIOSINTESIS</topic><topic>BIOSYNTHESE</topic><topic>Biosynthesis</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression regulation</topic><topic>GENETICA</topic><topic>GENETIQUE</topic><topic>Heterozygotes</topic><topic>Leaves</topic><topic>LIGASAS</topic><topic>LIGASE</topic><topic>Metabolism</topic><topic>Metabolism and Enzymology</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>NICOTIANA</topic><topic>Nitrogen metabolism</topic><topic>Overproduction</topic><topic>Percentages</topic><topic>Phenotypes</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>VIA BIOQUIMICA DEL METABOLISMO</topic><topic>VOIE BIOCHIMIQUE DU METABOLISME</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium)</creatorcontrib><creatorcontrib>Ghislain, M</creatorcontrib><creatorcontrib>Jacobs, M</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frankard, V. (Vrije Universiteit Brussel, Sint-Genesius Rode, Belgium)</au><au>Ghislain, M</au><au>Jacobs, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1992-08</date><risdate>1992</risdate><volume>99</volume><issue>4</issue><spage>1285</spage><epage>1293</epage><pages>1285-1293</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Lysine and threonine overproducer mutants in Nicotiana sylvestris, characterized by an altered regulation of, respectively, dihydrodipicolinate synthase and aspartate kinase activities, were crossed to assess the effects of the simultaneous presence of these genes on the biosynthesis of aspartate-derived amino acids. The monogenic dominant behavior of both resistance traits was confirmed, and their loci were found to be unlinked. Study of the inhibition properties of dihydrodipicolinate synthase and aspartate kinase activities in RAEC-1 X RLT 70 confirmed the heterozygote state of both mutations, because only half of their lysine-sensitive activity could still be inhibited by this negative effector. Analysis of the free amino acid pool during the growth of the double mutant revealed a major free lysine overproduction reaching up to 50% of the total pool, whereas the other aspartate-derived amino acids remained equally or even less abundant than in the wild type. An abnormal phenotype was clearly associated with such high levels of lysine accumulation, which points out the possible role of this amino acid in the developmental features of the plant. Comparison of the amino acid content, free and total (free + protein-bound), between the wild type, the two mutants, and the double mutant obtained by crossing them brings new insights on the regulation of the aspartate pathway, and on its implications in relationship to plant nutritional value improvement</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>16669034</pmid><doi>10.1104/pp.99.4.1285</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0032-0889 |
| ispartof | Plant physiology (Bethesda), 1992-08, Vol.99 (4), p.1285-1293 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_733494768 |
| source | JSTOR Archival Journals and Primary Sources Collection; Alma/SFX Local Collection |
| subjects | ACIDE AMINE ACIDE ASPARTIQUE ACIDO ASPARTICO ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino acids AMINOACIDOS Biological and medical sciences BIOSINTESIS BIOSYNTHESE Biosynthesis Enzymes Fundamental and applied biological sciences. Psychology Gene expression regulation GENETICA GENETIQUE Heterozygotes Leaves LIGASAS LIGASE Metabolism Metabolism and Enzymology MUTANT MUTANTES NICOTIANA Nitrogen metabolism Overproduction Percentages Phenotypes Plant physiology and development Plants TRANSFERASAS TRANSFERASE VIA BIOQUIMICA DEL METABOLISMO VOIE BIOCHIMIQUE DU METABOLISME |
| title | Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris |
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