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pyrroline/arabidopsis
Länken sparas på Urklipp
Sida 1 från 65 resultat
Synthesis and evaluation of effective inhibitors of plant δ1-pyrroline-5-carboxylate reductase.
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Analogues of previously studied phenyl-substituted aminomethylene-bisphosphonic acids were synthesized and evaluated as inhibitors of Arabidopsis thaliana δ(1)-pyrroline-5-carboxylate reductase. With the aim of improving their effectiveness, two main modifications were introduced into the inhibitory
Osmoregulation of a pyrroline-5-carboxylate reductase gene in Arabidopsis thaliana.
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In Arabidopsis thaliana (L.) Heynh. proline can account for up to 20% of the free amino acid pool after salt stress. Proline accumulation occurs in plants mainly by de novo synthesis from glutamate. The last step of the proline biosynthetic pathway is catalyzed by pyrroline-5-carboxylate (P5C)
A 69 bp fragment in the pyrroline-5-carboxylate reductase promoter of Arabidopsis thaliana activates minimal CaMV 35S promoter in a tissue-specific manner.
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The Arabidopsis thaliana gene that encodes pyrroline-5-carboxylate reductase (At-P5R), the last enzyme in proline biosynthesis in A. thaliana, is developmentally regulated and is highly expressed in cells that divide rapidly or undergo changes in osmotic potential. A 69 bp region (P69; -120 to -51)
Isolation and characterization of two different cDNAs of delta1-pyrroline-5-carboxylate synthase in alfalfa, transcriptionally induced upon salt stress.
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Two different cDNA clones, MsP5CS-1 and MsP5CS-2, encoding delta1 -pyrroline-5-carboxylate synthase (P5CS). the first enzyme of the proline biosynthetic pathway, were isolated from a lambdaZap-cDNA library constructed from salt stressed Medicago sativa roots. MsP5CS-1 (2.6 kb) has an open reading
Isolation, characterization, and chromosomal location of a gene encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana.
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A full-length cDNA and the corresponding At-P5S gene encoding the first enzyme of the proline biosynthetic pathway, the delta 1-pyrroline-5-carboxylate (P5C) synthetase, were isolated in Arabidopsis thaliana. The At-P5S cDNA encodes a protein of 717 amino acids showing high identity with the P5C
An Ancestral Allele of Pyrroline-5-carboxylate synthase1 Promotes Proline Accumulation and Drought Adaptation in Cultivated Barley.
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Water scarcity is a critical threat to global crop production. Here, we used the natural diversity of barley (Hordeum vulgare) to dissect the genetic control of proline (Pro) mediated drought stress adaptation. Genetic mapping and positional cloning of a major drought-inducible quantitative trait
Correlation between the induction of a gene for delta 1-pyrroline-5-carboxylate synthetase and the accumulation of proline in Arabidopsis thaliana under osmotic stress.
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The isolation and characterization is reported of a cDNA for delta 1-pyrroline-5-carboxylate (P5C) synthetase (cAtP5CS), an enzyme involved in the biosynthesis of proline, from a cDNA library prepared from a dehydrated rosette plant of Arabidopsis thaliana. Southern blot analysis suggested that only
Stress-responsive and developmental regulation of Delta(1)-pyrroline-5-carboxylate synthetase 1 (P5CS1) gene expression in Arabidopsis thaliana.
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Delta(1)-Pyrroline-5-carboxylate synthetase 1 (P5CS1) is the rate-limiting enzyme in the biosynthesis of proline by Arabidopsis thaliana. Results of Northern analysis using aba1, abi1, and abi3 mutants of A. thaliana suggest that the expression of the P5CS1 gene under water stress is induced via
Reciprocal regulation of delta 1-pyrroline-5-carboxylate synthetase and proline dehydrogenase genes controls proline levels during and after osmotic stress in plants.
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Plants generally accumulate free proline under osmotic stress conditions. Upon removal of the osmotic stress, the proline levels return to normal. In order to understand the mechanisms involved in regulating the levels of proline, we cloned and characterized a proline dehydrogenase (PDH) cDNA from
Role of proline and pyrroline-5-carboxylate metabolism in plant defense against invading pathogens.
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Pyrroline-5-carboxylate (P5C) is an intermediate product of both proline biosynthesis and catabolism. Recent evidences indicate that proline-P5C metabolism is tightly regulated in plants, especially during pathogen infection and abiotic stress. However, role of P5C and its metabolism in plants has
Δ1-Pyrroline-5-carboxylate reductase from Arabidopsis thaliana: stimulation or inhibition by chloride ions and feedback regulation by proline depend on whether NADPH or NADH acts as co-substrate.
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Δ(1)-pyrroline-5-carboxylate (P5C) reductase (P5CR) catalyses the final step of proline synthesis in plants. In Arabidopsis thaliana, protein levels are correlated neither to the corresponding mRNA copy numbers, nor to intracellular proline concentrations. The occurrence of post-translational
Isolation and characterization of a Δ1-pyrroline-5-carboxylate synthetase (NtP5CS) from Nitraria tangutorum Bobr. and functional comparison with its Arabidopsis homologue.
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Several functional and regulatory proteins play important roles in controlling plant stress tolerance. Proline (Pro) is one of the most accumulated osmolytes correlated with tolerance to stresses. Δ(1)-Pyrroline-5-carboxylate synthetase (P5CS) is a rate-limiting enzyme in Pro biosynthesis. In the
Developmental regulation of pyrroline-5-carboxylate reductase gene expression in Arabidopsis.
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At-P5R, a gene encoding the last enzyme of the proline (Pro) biosynthetic pathway in Arabidopsis thaliana, is developmentally regulated. To characterize the cis elements responsible for this developmental regulation, a series of 5' deletions of the At-P5R promoter were transcriptionally fused to a
Transcriptome changes in Arabidopsis thaliana infected with Pseudomonas syringae during drought recovery.
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Field-grown plants experience cycles of drought stress and recovery due to variation in soil moisture status. Physiological, biochemical and transcriptome responses instigated by recovery are expected to be different from drought stress and non-stressed state. Such responses can further aid or
Tailoring the structure of aminobisphosphonates to target plant P5C reductase.
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Using the structure of (3,5-dichlorophenyl)aminomethylenebisphosphonic acid as a lead compound, 25 new phosphonates were synthesized and evaluated as possible inhibitors of Arabidopsis thaliana delta1-pyrroline-5-carboxylate (P5C) reductase. Derivatives substituted in the phenyl ring retained the
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