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atriplex sagittata/نيكوتين

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مقالاتالتجارب السريريةبراءات الاختراع
15 النتائج

AhCMO, regulated by stresses in Atriplex hortensis, can improve drought tolerance in transgenic tobacco.

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Choline monooxygenase (CMO) catalyzes the committed step of glycine betaine (GlyBet) biosynthesis in many flowering plants. To investigate its effect on various stress tolerances in plant metabolic engineering, we isolated and characterized the CMO gene from Atriplex hortensis, a GlyBet natural

Stress proteins on the yeast cell surface determine resistance to osmotin, a plant antifungal protein.

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Strains of the yeast Saccharomyces cerevisiae differ in their sensitivities to tobacco osmotin, an antifungal protein of the PR-5 family. However, cells sensitive to tobacco osmotin showed resistance to osmotin-like proteins purified from the plant Atriplex nummularia, indicating a strict

Characterization of a DRE-binding transcription factor from a halophyte Atriplex hortensis.

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Environmental stresses, such as salinity, drought and cold, can induce the expression of a large amount of genes. Among these are many transcription factors that regulate the expression of downstream genes by specifically binding to cis-elements or forming transcriptional complexes with other

Plasma-membrane H(+)-ATPase gene expression is regulated by NaCl in cells of the halophyte Atriplex nummularia L.

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An Atriplex nummularia L. cDNA probe encoding the partial sequence of an isoform of the plasma-membrane H(+)-ATPase was isolated, and used to characterize the NaCl regulation of mRNA accumulation in cultured cells of this halophyte. The peptide (477 amino acids) translated from the open reading

Catabolism of adenine derivatives in leaves: study of the role of light on the in vivo activity of xanthine dehydrogenase.

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The in vivo activity of xanthine dehydrogenase (E.C. 1.2.1.37) was followed in leaf discs excised from illuminated or darkened plants. In cotyledons of Pharbitis nil, 24 hours of darkness enhanced the in vivo activity of xanthine dehydrogenase which increased between 2 to 5-fold depending on the
Two isoenzymes each of glucosephosphate isomerase (EC 5.3.1.9), phosphoglucomutase (EC 2.7.5.1), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.43) were separated by (NH4)2SO4 gradient solubilization and DEAE-cellulose ion-exchange chromatography from

AcEBP1, an ErbB3-Binding Protein (EBP1) from halophyte Atriplex canescens, negatively regulates cell growth and stress responses in Arabidopsis.

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An ErbB-3-binding protein gene AcEBP1, also known as proliferation-associated 2G4 gene (PA2G4s) belonging to the M24 superfamily, was obtained from the saltbush Atriplex canescens. Subcellular localization imaging showed the fusion protein AcEBP1-eGFP was located in the nucleus of epidermal cells in

Cell growth and water relations of the halophyte, Atriplex nummularia L., in response to NaCl.

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Growth reduction or cessation is an initial response of Atriplex nummularia L. cells to NaCl. However, A. nummularia L. cells that are adapted to 342 and 428 mM NaCl are capable of sustained growth in the presence of salt. Cells that are adapted to NaCl exhibit a reduced rate of division compared to

[Cloning and characterization of CMO gene from Atriplex hortensis].

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Glycine betaine is a widespread osmopretectant existed in many organisms. In higher plant, glycine betaine is synthesized via a two-sep oxidation reaction: choline-->betaine aldehyde-->glycine betaine. The first step, also the speed-limiting step, is catalyzed by choline monooxygenase(CMO). Choosing

AcPIP2, a plasma membrane intrinsic protein from halophyte Atriplex canescens, enhances plant growth rate and abiotic stress tolerance when overexpressed in Arabidopsis thaliana.

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CONCLUSIONS An aquaporin protein AcPIP2 from Atriplex canescens was involved in plant growth rate, abiotic stress tolerance in Arabidopsis. Under limited water condition, AcPIP2 leaded to the sensitivity to drought stress. An aquaporin protein (AcPIP2) was obtained from the saltbush Atriplex

Isolating the promoter of a stress-induced gene encoding betaine aldehyde dehydrogenase from the halophyte Atriplex centralasiatica Iljin.

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The betaine aldehyde dehydrogenase (AcBADH) gene of the halophyte Atriplex centralasiatica Iljin is induced by drought, salinity, cold stress and abscisic acid, in parallel with an increase in betaine level. In order to study the molecular basis of its expression and to obtain an effective

Expression of Osmotin-Like Genes in the Halophyte Atriplex nummularia L.

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A peptide (molecular mass 50 kilodaltons) that is immunologically related to tobacco osmotin was detected in cells of the halophyte Atriplex nummularia. This protein was constitutively expressed in both unadapted and NaCl-adapted cells. A predominant osmotin-like peptide (molecular mass 24

A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.

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Many heavy metals are essential for metabolic processes, but are toxic at elevated levels. Metal tolerance proteins provide resistance to this toxicity. In this study, we identified and characterized a heavy metal-associated protein, AcHMA1, from the halophyte, Atriplex canescens. Sequence analysis

AcERF2, an ethylene-responsive factor of Atriplex canescens, positively modulates osmotic and disease resistance in Arabidopsis thaliana.

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Ethylene-responsive factors (ERFs) comprise a large family of transcription factors in plants and play important roles in developmental processes and stress responses. Here, we characterized a novel AP2/ERF transcription factor, AcERF2, from the halophyte Atriplex canescens (four-wing saltbush,

NaCl regulation of plasma membrane H(+)-ATPase gene expression in a glycophyte and a halophyte.

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NaCl regulation of plasma membrane H(+)-ATPase gene expression in the glycophyte tobacco (Nicotiana tabacum L. var Wisconsin 38) and the halophyte Atriplex nummularia L. was evaluated by comparison of organ-specific mRNA abundance using homologous cDNA probes encoding the ATPases of the respective
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