Cd-Stress on Nitrogen Assimilation
Identifieur interne : 001887 ( Istex/Corpus ); précédent : 001886; suivant : 001888Cd-Stress on Nitrogen Assimilation
Auteurs : N. Boussama ; O. Ouariti ; A. Suzuki ; M. H. GhorbalSource :
- Journal of Plant Physiology [ 0176-1617 ] ; 1999.
English descriptors
- KwdEn :
Abstract
Summary: Nitrate assimilation in higher plants is the principal biosynthetic pathway leading to glutamate, required for synthesis of particular metabolites that participate in mechanisms of biochemical adaptation to heavy metal stress such as cadmium. Exposure of maize (Zea mays L.) seedlings to increasing cadmium concentrations for 12 days resulted in a significant decrease in nitrate content coupled to inhibition in activities of the enzymes nitrate reductase (EC 1.6.6.1), nitrite reductase (EC 1.6.6.4), glutamine synthetase (EC 6.3.1.2), ferredoxin-glutamate synthase (EC 1.4.7.1), and NADH-glutamate synthase (EC 1.4.1.14). Patterns of NADH- (aminating) and NAD+- (deaminating) glutamate dehydrogenase (EC 1.4.1.2) activities were opposed, with a great increase in the aminating direction. Concurrently, cadmium treatments promoted an increase in protease activity as well as accumulation of ammonia in tissues. These changes in enzyme activities were accompanied by a loss in total amino acids and proteins in both shoots and roots. However, of all amino acids quantified, glutamate, proline, lysine, methionine, and glycine showed a remarkable accumulation in cadmium treated plants, in comparison to control ones. The increased level of glutamate paralleled the elevated contents of γ-glutamylcysteine and glutathione in response to cadmium treatments. The magnitude of changes in all parameters investigated was concentration-dependent. Considered together, metabolite analysis and enzymatic measurements showed that cadmium induces a substantial shift in the operative pathways of ammonia assimilation, and suggested that the induction of NADH-glutamate dehydrogenase activity under cadmium stress may provide glutamate required for enhancing the synthesis of proline, γ-glutamylcysteine and glutathione, which is a common response to cadmium stress conditions. The possible association of these findings with cadmium-binding peptides is discussed.
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DOI: 10.1016/S0176-1617(99)80110-2
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<front><div type="abstract" xml:lang="en">Summary: Nitrate assimilation in higher plants is the principal biosynthetic pathway leading to glutamate, required for synthesis of particular metabolites that participate in mechanisms of biochemical adaptation to heavy metal stress such as cadmium. Exposure of maize (Zea mays L.) seedlings to increasing cadmium concentrations for 12 days resulted in a significant decrease in nitrate content coupled to inhibition in activities of the enzymes nitrate reductase (EC 1.6.6.1), nitrite reductase (EC 1.6.6.4), glutamine synthetase (EC 6.3.1.2), ferredoxin-glutamate synthase (EC 1.4.7.1), and NADH-glutamate synthase (EC 1.4.1.14). Patterns of NADH- (aminating) and NAD+- (deaminating) glutamate dehydrogenase (EC 1.4.1.2) activities were opposed, with a great increase in the aminating direction. Concurrently, cadmium treatments promoted an increase in protease activity as well as accumulation of ammonia in tissues. These changes in enzyme activities were accompanied by a loss in total amino acids and proteins in both shoots and roots. However, of all amino acids quantified, glutamate, proline, lysine, methionine, and glycine showed a remarkable accumulation in cadmium treated plants, in comparison to control ones. The increased level of glutamate paralleled the elevated contents of γ-glutamylcysteine and glutathione in response to cadmium treatments. The magnitude of changes in all parameters investigated was concentration-dependent. Considered together, metabolite analysis and enzymatic measurements showed that cadmium induces a substantial shift in the operative pathways of ammonia assimilation, and suggested that the induction of NADH-glutamate dehydrogenase activity under cadmium stress may provide glutamate required for enhancing the synthesis of proline, γ-glutamylcysteine and glutathione, which is a common response to cadmium stress conditions. The possible association of these findings with cadmium-binding peptides is discussed.</div>
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<term>glutamate dehydrogenase</term>
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<ce:author><ce:given-name>M.H.</ce:given-name>
<ce:surname>Ghorbal</ce:surname>
<ce:cross-ref refid="aff1"><ce:sup>1</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:affiliation id="aff1"><ce:label>1</ce:label>
<ce:textfn>Laboratoire de Physiologie Végétale «Nutrition et Métabolisme Azotés» (E 20/C 09), Département des Sciences Biologiques, Faculté des Sciences de Tunis, Campus Universitaire-1060 Tunis, Tunisia</ce:textfn>
</ce:affiliation>
<ce:affiliation id="aff2"><ce:label>2</ce:label>
<ce:textfn>Laboratoire du Métabolisme et de la Nutrition des Plantes, INRA, Route de Saint-Cyr, Versailles F-78026 Cedex, France</ce:textfn>
</ce:affiliation>
</ce:author-group>
<ce:date-received day="11" month="9" year="1998"></ce:date-received>
<ce:date-accepted day="2" month="2" year="1999"></ce:date-accepted>
<ce:abstract id="ab1" xml:lang="en"><ce:section-title>Summary</ce:section-title>
<ce:abstract-sec><ce:simple-para id="SP0005">Nitrate assimilation in higher plants is the principal biosynthetic pathway leading to glutamate, required for synthesis of particular metabolites that participate in mechanisms of biochemical adaptation to heavy metal stress such as cadmium. Exposure of maize (<ce:italic>Zea mays</ce:italic>
L.) seedlings to increasing cadmium concentrations for 12 days resulted in a significant decrease in nitrate content coupled to inhibition in activities of the enzymes nitrate reductase (EC 1.6.6.1), nitrite reductase (EC 1.6.6.4), glutamine synthetase (EC 6.3.1.2), ferredoxin-glutamate synthase (EC 1.4.7.1), and NADH-glutamate synthase (EC 1.4.1.14). Patterns of NADH- (aminating) and NAD<ce:sup>+</ce:sup>
- (deaminating) glutamate dehydrogenase (EC 1.4.1.2) activities were opposed, with a great increase in the aminating direction. Concurrently, cadmium treatments promoted an increase in protease activity as well as accumulation of ammonia in tissues. These changes in enzyme activities were accompanied by a loss in total amino acids and proteins in both shoots and roots. However, of all amino acids quantified, glutamate, proline, lysine, methionine, and glycine showed a remarkable accumulation in cadmium treated plants, in comparison to control ones. The increased level of glutamate paralleled the elevated contents of γ-glutamylcysteine and glutathione in response to cadmium treatments. The magnitude of changes in all parameters investigated was concentration-dependent. Considered together, metabolite analysis and enzymatic measurements showed that cadmium induces a substantial shift in the operative pathways of ammonia assimilation, and suggested that the induction of NADH-glutamate dehydrogenase activity under cadmium stress may provide glutamate required for enhancing the synthesis of proline, γ-glutamylcysteine and glutathione, which is a common response to cadmium stress conditions. The possible association of these findings with cadmium-binding peptides is discussed.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords class="keyword"><ce:section-title>Key words</ce:section-title>
<ce:keyword><ce:text>Zea mays</ce:text>
</ce:keyword>
<ce:keyword><ce:text>amino acids</ce:text>
</ce:keyword>
<ce:keyword><ce:text>cadmium stress</ce:text>
</ce:keyword>
<ce:keyword><ce:text>glutamate</ce:text>
</ce:keyword>
<ce:keyword><ce:text>glutathione</ce:text>
</ce:keyword>
<ce:keyword><ce:text>γ-glutamylcysteine</ce:text>
</ce:keyword>
<ce:keyword><ce:text>nitrate</ce:text>
</ce:keyword>
<ce:keyword><ce:text>nitrogen assimilating enzymes</ce:text>
</ce:keyword>
<ce:keyword><ce:text>proline</ce:text>
</ce:keyword>
</ce:keywords>
<ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title>
<ce:keyword><ce:text>γ-EC</ce:text>
<ce:keyword><ce:text>γ-glutamylcysteine</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>GDH</ce:text>
<ce:keyword><ce:text>glutamate dehydrogenase</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>GOGAT</ce:text>
<ce:keyword><ce:text>glutamate synthase</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>GS</ce:text>
<ce:keyword><ce:text>glutamine synthetase</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>GSH</ce:text>
<ce:keyword><ce:text>glutathione</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>NiR</ce:text>
<ce:keyword><ce:text>nitrite reductase</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>NR</ce:text>
<ce:keyword><ce:text>nitrate reductase</ce:text>
</ce:keyword>
</ce:keyword>
</ce:keywords>
</head>
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<mods version="3.6"><titleInfo lang="en"><title>Cd-Stress on Nitrogen Assimilation</title>
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<name type="personal"><namePart type="given">N.</namePart>
<namePart type="family">Boussama</namePart>
<affiliation>Laboratoire de Physiologie Végétale «Nutrition et Métabolisme Azotés» (E 20/C 09), Département des Sciences Biologiques, Faculté des Sciences de Tunis, Campus Universitaire-1060 Tunis, Tunisia</affiliation>
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<affiliation>Laboratoire de Physiologie Végétale «Nutrition et Métabolisme Azotés» (E 20/C 09), Département des Sciences Biologiques, Faculté des Sciences de Tunis, Campus Universitaire-1060 Tunis, Tunisia</affiliation>
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<name type="personal"><namePart type="given">A.</namePart>
<namePart type="family">Suzuki</namePart>
<affiliation>Laboratoire du Métabolisme et de la Nutrition des Plantes, INRA, Route de Saint-Cyr, Versailles F-78026 Cedex, France</affiliation>
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<name type="personal"><namePart type="given">M.H.</namePart>
<namePart type="family">Ghorbal</namePart>
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<abstract lang="en">Summary: Nitrate assimilation in higher plants is the principal biosynthetic pathway leading to glutamate, required for synthesis of particular metabolites that participate in mechanisms of biochemical adaptation to heavy metal stress such as cadmium. Exposure of maize (Zea mays L.) seedlings to increasing cadmium concentrations for 12 days resulted in a significant decrease in nitrate content coupled to inhibition in activities of the enzymes nitrate reductase (EC 1.6.6.1), nitrite reductase (EC 1.6.6.4), glutamine synthetase (EC 6.3.1.2), ferredoxin-glutamate synthase (EC 1.4.7.1), and NADH-glutamate synthase (EC 1.4.1.14). Patterns of NADH- (aminating) and NAD+- (deaminating) glutamate dehydrogenase (EC 1.4.1.2) activities were opposed, with a great increase in the aminating direction. Concurrently, cadmium treatments promoted an increase in protease activity as well as accumulation of ammonia in tissues. These changes in enzyme activities were accompanied by a loss in total amino acids and proteins in both shoots and roots. However, of all amino acids quantified, glutamate, proline, lysine, methionine, and glycine showed a remarkable accumulation in cadmium treated plants, in comparison to control ones. The increased level of glutamate paralleled the elevated contents of γ-glutamylcysteine and glutathione in response to cadmium treatments. The magnitude of changes in all parameters investigated was concentration-dependent. Considered together, metabolite analysis and enzymatic measurements showed that cadmium induces a substantial shift in the operative pathways of ammonia assimilation, and suggested that the induction of NADH-glutamate dehydrogenase activity under cadmium stress may provide glutamate required for enhancing the synthesis of proline, γ-glutamylcysteine and glutathione, which is a common response to cadmium stress conditions. The possible association of these findings with cadmium-binding peptides is discussed.</abstract>
<subject lang="en"><genre>Key words</genre>
<topic>Zea mays</topic>
<topic>amino acids</topic>
<topic>cadmium stress</topic>
<topic>glutamate</topic>
<topic>glutathione</topic>
<topic>γ-glutamylcysteine</topic>
<topic>nitrate</topic>
<topic>nitrogen assimilating enzymes</topic>
<topic>proline</topic>
</subject>
<subject lang="en"><genre>Abbreviations</genre>
<topic>γ-EC : γ-glutamylcysteine</topic>
<topic>GDH : glutamate dehydrogenase</topic>
<topic>GOGAT : glutamate synthase</topic>
<topic>GS : glutamine synthetase</topic>
<topic>GSH : glutathione</topic>
<topic>NiR : nitrite reductase</topic>
<topic>NR : nitrate reductase</topic>
</subject>
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<originInfo><dateIssued encoding="w3cdtf">199909</dateIssued>
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