Source:http://linkedlifedata.com/resource/pubmed/id/12631328
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-3-12
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pubmed:abstractText |
Legumes acquire significant amounts of nitrogen for growth from symbiotic nitrogen fixation. The glutamine synthetase (GS)/NADH-dependent glutamate synthase (NADH-GOGAT) cycle catalyzes initial nitrogen assimilation. This report describes the impact of specifically reducing nodule NADH-GOGAT activity on symbiotic performance of alfalfa (Medicago sativa L.). Four independent transgenic alfalfa lines, designated GA89, GA87, GA88, and GA82 (for GOGATantisense), containing an antisense NADH-GOGAT cDNA fragment under the control of the soybean leghemoglobin (lbc3) promoter were evaluated. The GA plants were fertile and showed normal growth in non-symbiotic conditions. The NADH-GOGAT antisense transgene was heritable and the T1 plants showed phenotypic alterations - similar to primary transformants. Clonally propagated plants were inoculated with Sinorhizobium meliloti after rooting and the symbiotic phenotype was analyzed 21 days post-inoculation. Nodules of each GA line had reduced NADH-GOGAT activity, ranging from 33 to 87% of control plants, that was accompanied by comparable decreases in RNA and protein. Plants from the GA89 line, with the lowest NADH-GOGAT activity (c. 30%), presented a strikingly altered symbiotic phenotype: concomitantly activities of key enzyme for carbon and nitrogen assimilation decreased; nodule amino acids and amides were reduced while sucrose accumulated. Antisense GOGAT plants were chlorotic, reduced in fresh weight, and had a lower N content than control plants. Photosynthesis was also impaired in antisense plants. Specifically, reducing NADH-GOGAT in nodules resulted in plants having impaired nitrogen assimilation and altered carbon/nitrogen metabolic flux.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Antisense Elements (Genetics),
http://linkedlifedata.com/resource/pubmed/chemical/Carbon,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Synthase (NADH),
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1037-49
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12631328-Amino Acid Oxidoreductases,
pubmed-meshheading:12631328-Antisense Elements (Genetics),
pubmed-meshheading:12631328-Carbon,
pubmed-meshheading:12631328-Gene Expression Regulation, Plant,
pubmed-meshheading:12631328-Glutamate Synthase (NADH),
pubmed-meshheading:12631328-Medicago sativa,
pubmed-meshheading:12631328-Mycorrhizae,
pubmed-meshheading:12631328-Nitrogen,
pubmed-meshheading:12631328-Phenotype,
pubmed-meshheading:12631328-Plants, Genetically Modified,
pubmed-meshheading:12631328-Symbiosis
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pubmed:year |
2003
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pubmed:articleTitle |
Antisense inhibition of NADH glutamate synthase impairs carbon/nitrogen assimilation in nodules of alfalfa (Medicago sativa L.).
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pubmed:affiliation |
Centro de Investigación sobre Fijación de Nitrógeno, UNAM, Ap. Postal 565-A, Cuernavaca, Mor. México.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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