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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-2-14
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pubmed:abstractText |
The physiological role of the NADH-dependent glutamine-2-oxoglutarate aminotransferase (NADH-GOGAT) enzyme was addressed in Arabidopsis using gene expression analysis and by the characterization of a knock-out T-DNA insertion mutant (glt1-T) in the single NADH-GOGAT GLT1 gene. The NADH-GOGAT GLT1 mRNA is expressed at higher levels in roots than in leaves. This expression pattern contrasts with GLU1, the major gene encoding Fd-GOGAT, which is most highly expressed in leaves and is involved in photorespiration. These distinct organ-specific expression patterns suggested a non-redundant physiological role for the NADH-GOGAT and Fd-GOGAT gene products. To test the in vivo function of NADH-GOGAT, we conducted molecular and physiological analysis of the glt1-T mutant, which is null for NADH-GOGAT, as judged by mRNA level and enzyme activity. Metabolic analysis showed that the glt1-T mutant has a specific defect in growth and glutamate biosynthesis when photorespiration was repressed by 1% CO2. Under these conditions, the glt1-T mutant displayed a 20% decrease in growth and a dramatic 70% reduction in glutamate levels. Herein, we discuss the significance of NADH-GOGAT in non-photorespiratory ammonium assimilation and in glutamate synthesis required for plant development.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyll,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Synthase (NADH),
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/T-DNA,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate synthase (ferredoxin)
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0960-7412
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
347-58
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11844111-Amino Acid Oxidoreductases,
pubmed-meshheading:11844111-Amino Acids,
pubmed-meshheading:11844111-Arabidopsis,
pubmed-meshheading:11844111-Carbon Dioxide,
pubmed-meshheading:11844111-Chlorophyll,
pubmed-meshheading:11844111-DNA, Bacterial,
pubmed-meshheading:11844111-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11844111-Gene Expression Regulation, Plant,
pubmed-meshheading:11844111-Glutamate Synthase (NADH),
pubmed-meshheading:11844111-Glutamic Acid,
pubmed-meshheading:11844111-Glutamine,
pubmed-meshheading:11844111-Light,
pubmed-meshheading:11844111-Mutagenesis, Insertional,
pubmed-meshheading:11844111-Mutation,
pubmed-meshheading:11844111-Oxygen Consumption,
pubmed-meshheading:11844111-Phenotype,
pubmed-meshheading:11844111-Plant Leaves,
pubmed-meshheading:11844111-Plant Roots,
pubmed-meshheading:11844111-Quaternary Ammonium Compounds,
pubmed-meshheading:11844111-RNA, Messenger
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pubmed:year |
2002
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pubmed:articleTitle |
Arabidopsis glt1-T mutant defines a role for NADH-GOGAT in the non-photorespiratory ammonium assimilatory pathway.
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pubmed:affiliation |
Department of Biology, New York University, 100 Washington Square East, 1009 Main Building, New York, NY 10003, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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