Source:http://linkedlifedata.com/resource/pubmed/id/20444205
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rdf:type | |
lifeskim:mentions |
umls-concept:C0003995,
umls-concept:C0011155,
umls-concept:C0013443,
umls-concept:C0017801,
umls-concept:C0022173,
umls-concept:C0028158,
umls-concept:C0040715,
umls-concept:C0178784,
umls-concept:C0596076,
umls-concept:C0596988,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0936012,
umls-concept:C1138842,
umls-concept:C1383501,
umls-concept:C1522702
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pubmed:issue |
9
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pubmed:dateCreated |
2010-11-5
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pubmed:abstractText |
Nitrogen (N) metabolism was characterized in the developing ear of glutamine synthetase deficient mutants (gln1-3, gln1-4 and gln1-3/gln1-4) of maize exhibiting a reduction in kernel yield. During the grain-filling period, the metabolite contents, enzyme activities and steady-state levels of transcripts for marker genes of amino acid synthesis and interconversion were monitored in the cob and kernels. The ear of gln1-3 and gln1-3/gln1-4 had a higher free amino acid content and a lower C/N ratio, when compared to the wild type. The free ammonium concentrations were also much higher in gln1-3/gln1-4, and Asn accumulation was higher in gln1-3 and gln1-3/gln1-4. The level of transcripts of ZmAS3 and ZmAS4, two genes encoding asparagine synthetase, increased in the 'aborted kernels' of gln1-3 and gln1-3/gln1-4. The results show that N metabolism is clearly different in developing and 'aborted kernels'. The data support the hypothesis that N accumulated in 'aborted kernels' is remobilized via the cob to developing kernels using Asn as a transport molecule. The two genes ZmAS3 and ZmAS4 are likely to play an important role during this process.
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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/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1467-7652
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pubmed:author | |
pubmed:copyrightInfo |
© 2010 INRA. Plant Biotechnology Journal © 2010 Society for Experimental Biology and Blackwell Publishing Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
966-78
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pubmed:meshHeading |
pubmed-meshheading:20444205-Asparagine,
pubmed-meshheading:20444205-Biological Transport,
pubmed-meshheading:20444205-Cytosol,
pubmed-meshheading:20444205-Gene Expression Regulation, Plant,
pubmed-meshheading:20444205-Glutamate-Ammonia Ligase,
pubmed-meshheading:20444205-Isoenzymes,
pubmed-meshheading:20444205-Mutation,
pubmed-meshheading:20444205-Nitrogen,
pubmed-meshheading:20444205-Plant Proteins,
pubmed-meshheading:20444205-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20444205-Zea mays
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pubmed:year |
2010
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pubmed:articleTitle |
Analysis of amino acid metabolism in the ear of maize mutants deficient in two cytosolic glutamine synthetase isoenzymes highlights the importance of asparagine for nitrogen translocation within sink organs.
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pubmed:affiliation |
Unité de Nutrition Azotée des Plantes, Unité de Recherche 511, Institut Jean-Pierre Bourgin, Institut National de la Recherche Agronomique, Centre de Versailles-Grignon, Versailles Cedex, France.
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pubmed:publicationType |
Journal Article
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