l arginine/arabidopsis

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Arabidopsis chloroplasts dissimilate L-arginine and L-citrulline for use as N source.

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When aseptically grown on defined medium with either L-arginine, L-citrulline, or nitrate as the sole N source, Arabidopsis plants grew and developed normally. Three catabolic activities, L-arginine iminohydrolase, L-ornithine carbamoyltransferase, and carbamate kinase, were found in stromal

PsbY, a novel manganese-binding, low-molecular-mass protein associated with photosystem II.

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We describe two related manganese-binding polypeptides with L-arginine metabolizing enzyme activity that can be detected as distinct components (designated PsbY-A1 and PsbY-A2, previously called L-AME) in membranes containing Photosystem II (PS II) from spinach. The polypeptides are bitopic and

Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana.

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A cDNA encoding a homolog of mammalian serine racemase, a unique enzyme in eukaryotes, was isolated from Arabidopsis thaliana and expressed in Escherichia coli cells. The gene product, of which the amino acid residues for binding pyridoxal 5'-phosphate (PLP) are conserved in this as well as

Nitric oxide acts downstream of auxin to trigger root ferric-chelate reductase activity in response to iron deficiency in Arabidopsis.

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In response to iron (Fe) deficiency, dicots employ a reduction-based mechanism by inducing ferric-chelate reductase (FCR) at the root plasma membrane to enhance Fe uptake. However, the signal pathway leading to FCR induction is still unclear. Here, we found that the Fe-deficiency-induced increase of

Exogenous auxin-induced NO synthesis is nitrate reductase-associated in Arabidopsis thaliana root primordia.

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Nitric oxide (NO) functions in various physiological and developmental processes in plants. However, the source of this signaling molecule in the diversity of plant responses is not well understood. It is known that NO mediates auxin-induced adventitious and lateral root (LR) formation. In this

Salt stress reduces root meristem size by nitric oxide-mediated modulation of auxin accumulation and signaling in Arabidopsis.

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The development of the plant root system is highly plastic, which allows the plant to adapt to various environmental stresses. Salt stress inhibits root elongation by reducing the size of the root meristem. However, the mechanism underlying this process remains unclear. In this study, we explored

Involvement of nitrate reductase (NR) in osmotic stress-induced NO generation of Arabidopsis thaliana L. roots.

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Nitric oxide (NO) is undoubtedly a potential signal molecule in diverse developmental processes and stress responses. Despite our extensive knowledge about the role of NO in physiological and stress responses, the source of this gaseous molecule is still unresolved. The aim of this study was to

Interference with the citrulline-based nitric oxide synthase assay by argininosuccinate lyase activity in Arabidopsis extracts.

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There are many reports of an arginine-dependent nitric oxide synthase activity in plants; however, the gene(s) or protein(s) responsible for this activity have yet to be convincingly identified. To measure nitric oxide synthase activity, many studies have relied on a citrulline-based assay that

NITRIC OXIDE SYNTHASE INHIBITOR L-NAME AFFECTS ARABIDOPSIS ROOT GROWTH, MORPHOLOGY AND MICROTUBULE ORGANIZATION.

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The presence of evolutionarily conserved NOS or NOS-like enzymes in land plants different than those in animals is still unclear, despite their activity has been revealed in cytosol and some organelles. At the same time, the emerging evidence for the importance of L-arginine-dependent pathways of NO

Root uptake of cationic amino acids by Arabidopsis depends on functional expression of amino acid permease 5.

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* Specific transporters mediate uptake of amino acids by plant roots. Earlier studies have indicated that the lysine histidine transporter 1 and amino acid permease 1 participate in this process, but although plant roots have been shown to absorb cationic amino acids with high affinity, neither of

Study of oligogalacturonides-triggered nitric oxide (NO) production provokes new questioning about the origin of NO biosynthesis in plants.

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We investigated the production and function of nitric oxide (NO) in Arabidopsis thaliana leaf discs as well as whole plants elicited by oligogalacturonides (OGs). Using genetic, biochemical and pharmacological approaches, we provided evidence that OGs induced a Nitrate Reductase (NR)-dependent NO

Transcription factor sensor system for parallel quantification of metabolites on-chip.

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Steadily growing demands for identification and quantification of cellular metabolites in higher throughput have brought a need for new analytical technologies. Here, we developed a synthetic biological sensor system for quantifying metabolites from biological cell samples. For this, bacterial

Inhibition of NO Biosynthetic Activities during Rehydration of Ramalina farinacea Lichen Thalli Provokes Increases in Lipid Peroxidation.

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Lichens are poikilohydrous symbiotic associations between a fungus, photosynthetic partners, and bacteria. They are tolerant to repeated desiccation/rehydration cycles and adapted to anhydrobiosis. Nitric oxide (NO) is a keystone for stress tolerance of lichens; during lichen rehydration, NO limits

SNF1-related protein kinases type 2 are involved in plant responses to cadmium stress.

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Cadmium ions are notorious environmental pollutants. To adapt to cadmium-induced deleterious effects plants have developed sophisticated defense mechanisms. However, the signaling pathways underlying the plant response to cadmium are still elusive. Our data demonstrate that SnRK2s (for SNF1-related

Nitric oxide affects seed oil accumulation and fatty acid composition through protein S-nitrosation

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Nitric oxide (NO) has been implicated as a key signaling molecule involved in a wide spectrum of plant developmental and stress responses. Here, we found that NO also played important role in seed oil content and fatty acid composition. RNAi silencing Arabidopsis thaliana S-nitrosoglutathione

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