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1.
Physiol Plant ; 147(3): 261-9, 2013 Mar.
Article in English | MEDLINE | ID: mdl-22901048

ABSTRACT

Trehalose is a non-reducing disaccharide involved in stress tolerance in plants. To understand better the role of trehalose in the osmotic stress response in linseed (Linum usitatissimum), trehalose content in leaves was studied. First, the method commonly used for sugar determination, high performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD), gave unsatisfactory results and the separation efficiency could not be improved by varying the elution conditions. The same problem was also found in the model plant: Arabidopsis thaliana. After clearly highlighting a co-elution of trehalose in these two species by a trehalase assay and liquid chromatography-high resolution mass spectrometry analysis, gas chromatography-mass spectrometry (GC-MS) was used as the analytical method instead. These results confirmed that trehalose content is currently overestimated by HPAEC-PAD analysis, approximately 7 and 13 times for A. thaliana and linseed respectively. Thus GC-MS gave more satisfactory results for trehalose quantification in plants. With this method, trehalose accumulation was observed in linseed during an osmotic stress (-0.30 MPa), the quantity (31.49 nmol g(-1) dry weight after 48 h) appears too low to assign an osmoprotector or osmoregulator role to trehalose in stressed linseed.


Subject(s)
Flax/metabolism , Gas Chromatography-Mass Spectrometry/methods , Trehalose/analysis , Arabidopsis/metabolism , Chromatography, High Pressure Liquid , Chromatography, Ion Exchange , Flax/physiology , Glucose/analysis , Glucose/metabolism , Liquid-Liquid Extraction , Osmosis , Plant Extracts/analysis , Plant Leaves/metabolism , Trehalase/metabolism , Trehalose/metabolism
2.
Trends Plant Sci ; 15(7): 409-17, 2010 Jul.
Article in English | MEDLINE | ID: mdl-20494608

ABSTRACT

The disaccharide trehalose is involved in stress response in many organisms. However, in plants, its precise role remains unclear, although some data indicate that trehalose has a protective role during abiotic stresses. By contrast, some trehalose metabolism mutants exhibit growth aberrations, revealing potential negative effects on plant physiology. Contradictory effects also appear under biotic stress conditions. Specifically, trehalose is essential for the infectivity of several pathogens but at the same time elicits plant defense. Here, we argue that trehalose should not be regarded only as a protective sugar but rather like a double-faced molecule and that further investigation is required to elucidate its exact role in stress tolerance in plants.


Subject(s)
Plants/metabolism , Stress, Physiological , Trehalose/metabolism , Animals , Apoptosis , Humans , Plant Cells , Plants/microbiology , Symbiosis , Trehalose/chemistry
3.
Plant Cell ; 18(11): 3252-74, 2006 Nov.
Article in English | MEDLINE | ID: mdl-17138698

ABSTRACT

The roles of two cytosolic maize glutamine synthetase isoenzymes (GS1), products of the Gln1-3 and Gln1-4 genes, were investigated by examining the impact of knockout mutations on kernel yield. In the gln1-3 and gln1-4 single mutants and the gln1-3 gln1-4 double mutant, GS mRNA expression was impaired, resulting in reduced GS1 protein and activity. The gln1-4 phenotype displayed reduced kernel size and gln1-3 reduced kernel number, with both phenotypes displayed in gln1-3 gln1-4. However, at maturity, shoot biomass production was not modified in either the single mutants or double mutants, suggesting a specific impact on grain production in both mutants. Asn increased in the leaves of the mutants during grain filling, indicating that it probably accumulates to circumvent ammonium buildup resulting from lower GS1 activity. Phloem sap analysis revealed that unlike Gln, Asn is not efficiently transported to developing kernels, apparently causing reduced kernel production. When Gln1-3 was overexpressed constitutively in leaves, kernel number increased by 30%, providing further evidence that GS1-3 plays a major role in kernel yield. Cytoimmunochemistry and in situ hybridization revealed that GS1-3 is present in mesophyll cells, whereas GS1-4 is specifically localized in the bundle sheath cells. The two GS1 isoenzymes play nonredundant roles with respect to their tissue-specific localization.


Subject(s)
Cytosol/enzymology , Edible Grain/economics , Edible Grain/enzymology , Glutamate-Ammonia Ligase/metabolism , Isoenzymes/metabolism , Zea mays/enzymology , Amino Acid Sequence , Base Sequence , Gene Expression Regulation, Enzymologic , Gene Expression Regulation, Plant , Genome, Plant/genetics , Glutamate-Ammonia Ligase/chemistry , Glutamate-Ammonia Ligase/genetics , Glutamate-Ammonia Ligase/isolation & purification , Isoenzymes/chemistry , Isoenzymes/genetics , Isoenzymes/isolation & purification , Molecular Sequence Data , Mutagenesis, Insertional , Mutation/genetics , Phenotype , Phloem/enzymology , Plant Leaves/cytology , Plant Leaves/enzymology , Plant Leaves/ultrastructure , Plant Roots/cytology , Plant Roots/enzymology , Plant Shoots/enzymology , Protein Subunits/chemistry , Protein Subunits/genetics , Protein Subunits/isolation & purification , Protein Subunits/metabolism , Protein Transport , Proteomics , RNA, Messenger/genetics , RNA, Messenger/metabolism , Transcription, Genetic , Xylem/enzymology , Zea mays/cytology , Zea mays/ultrastructure
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