Document Detail


Changes in the cellular and subcellular localization of glutamine synthetase and glutamate dehydrogenase during flag leaf senescence in wheat (Triticum aestivum L.).
MedLine Citation:
PMID:  15840646     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In order to improve our understanding of the regulation of nitrogen assimilation and recycling in wheat (Triticum aestivum L.), we studied the localization of plastidic (GS2) and cytosolic (GS1) glutamine synthetase isoenzymes and of glutamate dehydrogenase (GDH) during natural senescence of the flag leaf and in the stem. In mature flag leaves, large amounts of GS1 were detected in the connections between the mestome sheath cells and the vascular cells, suggesting an active transfer of nitrogen organic molecules within the vascular system in the mature flag leaf. Parallel to leaf senescence, an increase of a GS1 polypeptide (GS1b) was detected in the mesophyll cytosol of senescing leaves, while the GS protein content represented by another polypetide (GS1a) in the phloem companion cells remained practically constant in both leaves and stems. Both GDH aminating activity and protein content were strongly induced in senescing flag leaves. The induction occurred both in the mitochondria and in the cytosol of phloem companion cells, suggesting that the shift in GDH cellular compartmentation is important during leaf nitrogen remobilization although the metabolic or sensing role of the enzyme remains to be elucidated. Taken together, our results suggest that in wheat, nitrogen assimilation and recycling are compartmentalized between the mesophyll and the vasculature, and are shifted in different cellular compartments within these two tissues during the transition of sink leaves to source leaves.
Authors:
Thomas Kichey; Jacques Le Gouis; Brigitte Sangwan; Bertrand Hirel; Frédéric Dubois
Related Documents :
16055186 - Evaluation of manisa propolis effect on leukemia cell line by telomerase activity.
2919136 - Quantitative histology of cartilage cell columns in the human costochondral junction: f...
8114516 - Serine/threonine protein kinases and calcium-dependent protease in senescent imr-90 fib...
11976216 - Frequent intracellular clonal expansions of somatic mtdna mutations: significance and m...
3309476 - Mathematical models for a g0 phase in saccharomyces cerevisiae.
20856206 - Blocking wnt signaling by sfrp-like molecules inhibits in vivo cell proliferation and t...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-04-19
Journal Detail:
Title:  Plant & cell physiology     Volume:  46     ISSN:  0032-0781     ISO Abbreviation:  Plant Cell Physiol.     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-07-04     Completed Date:  2005-09-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9430925     Medline TA:  Plant Cell Physiol     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  964-74     Citation Subset:  IM    
Affiliation:
Laboratoire d'Androgenèse et Biotechnologie Végétale, Université de Picardie Jules Verne, 33, Rue saint-Leu, 80039 Amiens Cedex, France.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cytosol / enzymology
Glutamate Dehydrogenase / metabolism*
Glutamate-Ammonia Ligase / metabolism*
Isoenzymes / metabolism
Microscopy, Immunoelectron
Nitrogen / metabolism
Plant Leaves / cytology,  enzymology,  growth & development
Plant Stems / cytology,  enzymology,  growth & development
Plastids / enzymology
Subcellular Fractions / enzymology
Triticum / cytology,  enzymology*,  growth & development*
Chemical
Reg. No./Substance:
0/Isoenzymes; 7727-37-9/Nitrogen; EC 1.4.1.2/Glutamate Dehydrogenase; EC 6.3.1.2/Glutamate-Ammonia Ligase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The lysine-rich arabinogalactan-protein subfamily in Arabidopsis: gene expression, glycoprotein puri...
Next Document:  PECAM-1, alpha6 integrins and neutrophil elastase cooperate in mediating neutrophil transmigration.