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cystathionine/arabidopsis thaliana
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Crystal structure of the single cystathionine β-synthase domain-containing protein CBSX1 from Arabidopsis thaliana.
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The single cystathionine β-synthase (CBS) pair proteins from Arabidopsis thaliana have been identified as being a redox regulator of the thioredoxin (Trx) system. CBSX1 and CBSX2, which are two of the six Arabidopsis cystathione β-synthase domain-containing proteins that contain only a single CBS
Concurrent Overexpression of Arabidopsis thaliana Cystathionine γ-Synthase and Silencing of Endogenous Methionine γ-Lyase Enhance Tuber Methionine Content in Solanum tuberosum.
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Potatoes (Solanum tuberosum) are deficient in methionine, an essential amino acid in human and animal diets. Higher methionine levels increase the nutritional quality and promote the typically pleasant aroma associated with baked and fried potatoes. Several attempts have been made to elevate tuber
Cloning of an Arabidopsis thaliana cDNA encoding cystathionine beta-lyase by functional complementation in Escherichia coli.
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Cystathionine beta-lyase, the second enzyme involved in the methionine biosynthetic pathway in plants, catalyses the synthesis of homocysteine from cystathionine. A cDNA encoding cystathionine beta-lyase was cloned from an Arabidopsis thaliana expression library by complementation of an Escherichia
Decay kinetics of autogenously regulated CGS1 mRNA that codes for cystathionine gamma-synthase in Arabidopsis thaliana.
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Cystathionine gamma-synthase (CGS) catalyses the first committed step in methionine (Met) biosynthesis in higher plants. Stability of CGS1 mRNA encoding CGS in Arabidopsis thaliana is regulated by negative feedback in response to Met application and the amino acid sequence of CGS itself acts in cis
Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli.
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Cystathionine beta-lyase is a key enzyme in sulphur metabolism that catalyses the second reaction specific for methionine biosynthesis, the pyridoxal 5'-phosphate-dependent beta-cleavage of cystathionine to produce homocysteine. To obtain insight into the biochemical properties of the plant enzyme,
The first exon coding region of cystathionine gamma-synthase gene is necessary and sufficient for downregulation of its own mRNA accumulation in transgenic Arabidopsis thaliana.
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Expression of the gene for cystathionine gamma-synthase (CGS), which catalyzes the key step of methionine biosynthesis, is feedback regulated at the level of mRNA stability. The first exon polypeptide of CGS is suggested to be involved in this regulation and amino acid sequence alterations caused by
Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.
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A cDNA clone, CGS1, encoding cystathionine gamma-synthase (CGS) from Arabidopsis thaliana was selected by complementation of CGS mutant strain of Escherichia coli (metB). Cells expressing CGS1 can grow on medium lacking Met and contain CGS enzyme activity. Genomic DNA blot analysis of A. thaliana
Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli.
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Cystathionine gamma-synthase catalyses the first reaction specific for methionine biosynthesis in plants, the gamma-replacement of the phosphoryl substituent of O-phosphohomoserine by cysteine. A cDNA encoding cystathionine gamma-synthase from Arabidopsis thaliana has been cloned and used to
Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana.
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Cystathione beta-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as
S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis.
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Cystathionine gamma-synthase, the first committed enzyme of methionine biosynthesis in higher plants, is encoded by the CGS1 gene in Arabidopsis thaliana. We have shown previously that the stability of the CGS1 mRNA is negatively regulated in response to methionine application [Chiba, Y., Ishikawa,
Overexpression of cystathionine-gamma-synthase enhances selenium volatilization in Brassica juncea.
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Selenium (Se) can be assimilated and volatilized via the sulfate assimilation pathway. Cystathionine-gamma-synthase (CGS) is thought to catalyze the synthesis of Se-cystathionine from Se-cysteine, the first step in the conversion of Se-cysteine to volatile dimethylselenide. Here the hypothesis was
Identification of cystathionine γ-synthase and threonine synthase from Cicer arietinum and Lens culinaris.
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In plants, cystathionine γ-synthase (CGS) and threonine synthase (TS) compete for the branch-point metabolite O-phospho-L-homoserine. These enzymes are potential targets for metabolic engineering studies, aiming to alter the flux through the competing methionine and threonine biosynthetic pathways,
Repression of CYSTATHIONINE γ-SYNTHASE in Seeds Recruits the S-Methylmethionine Cycle.
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S-Methylmethionine (SMM) was suggested previously to participate in the metabolism of methionine (Met) in seeds. To further reveal its roles, we had previously produced transgenic Arabidopsis (Arabidopsis thaliana) RNA interference (RNAi) seeds with lower transcript expression of CYSTATHIONINE
The N-terminal cleavable pre-sequence encoded in the first exon of cystathionine γ-synthase contains two different functional domains for chloroplast targeting and regulation of gene expression.
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Chloroplast transit peptide sequences (cTPs) located in the N-terminal region of nuclear-encoded chloroplast proteins are essential for their sorting, and are generally cleaved from the proteins after their import into the chloroplasts. The Arabidopsis thaliana cystathionine γ-synthase (CGS), the
In vivo analysis of various substrates utilized by cystathionine gamma-synthase and O-acetylhomoserine sulfhydrylase in methionine biosynthesis.
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To gain insight into the evolution of the methionine biosynthesis pathway, in vivo complementation tests were performed. The substrate specificity of three enzymes that intrinsically use different homoserine-esterified substrates and have different sulfur assimilation pathways was examined: two
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