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biotin/arabidopsis thaliana
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Biotin synthesis in higher plants: purification and characterization of bioB gene product equivalent from Arabidopsis thaliana overexpressed in Escherichia coli and its subcellular localization in pea leaf cells.
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Biotin synthase catalyses the final step in the biotin biosynthetic pathway and is encoded by the bioB gene in Escherichia coli. To investigate the conversion of dethiobiotin to biotin in the plant kingdom, the cDNA encoding the bioB gene product equivalent from Arabidopsis thaliana was used to
Evidence for multiple forms of biotin holocarboxylase synthetase in pea (Pisum sativum) and in Arabidopsis thaliana: subcellular fractionation studies and isolation of a cDNA clone.
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The intracellular compartmentation of biotin holocarboxylase synthetase has been investigated in pea (Pisum sativum) leaves, by isolation of organelles and fractionation of protoplasts. Enzyme activity was mainly located in cytosol (approx. 90% of total cellular activity). Significant activity was
Purification and properties of the chloroplastic form of biotin holocarboxylase synthetase from Arabidopsis thaliana overexpressed in Escherichia coli.
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Holocarboxylase synthetases (HCSs) are key enzymes in biotin utilisation in both prokaryotes and eukaryotes. In a previous study, we demonstrated that, in plants, HCS activity is localised in cytosol, chloroplasts and mitochondria. We also described the cloning and sequencing of a full-length cDNA
Arrested Embryos from the bio1 Auxotroph of Arabidopsis thaliana Contain Reduced Levels of Biotin.
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The bio1 auxotroph of Arabidopsis thaliana is a recessive embryonic lethal that forms normal plants in the presence of biotin. The purpose of this study was to determine whether aborted seeds produced by heterozygous plants grown without vitamin supplements contained reduced levels of biotin. Two
Characterization of the cDNA and gene coding for the biotin synthase of Arabidopsis thaliana.
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Biotin, an essential cofactor, is synthesized de novo only by plants and some microbes. An Arabidopsis thaliana expressed sequence tag that shows sequence similarity to the carboxyl end of biotin synthase from Escherichia coli was used to isolate a near-full-length cDNA. This cDNA was shown to code
Complementation of an Arabidopsis thaliana biotin auxotroph with an Escherichia coli biotin biosynthetic gene.
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The Arabidopsis thaliana biotin auxotroph biol was rendered prototrophic by transformation with a chimeric transgene containing the Escherichia coli bio A gene driven by a constitutive promoter. The bio A gene encodes the biotin biosynthetic enzyme 7, 8-diaminopelargonic acid aminotransferase.
Biotin synthase from Arabidopsis thaliana. cDNA isolation and characterization of gene expression.
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The full-length BIO2 cDNA from Arabidopsis thaliana was isolated using an expressed sequence tag that was homologous to the Escherichia coli biotin synthase gene (BioB). Comparisons of the deduced amino acid sequence from BIO2 with bacterial and yeast biotin synthase homologs revealed a high degree
Structure of the CAC1 gene and in situ characterization of its expression. The Arabidopsis thaliana gene coding for the biotin-containing subunit of the plastidic acetyl-coenzyme A carboxylase.
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The CAC1 gene of Arabidopsis thaliana that codes for the biotin carboxyl-carrier subunit of the heteromeric acetyl-coenzyme A carboxylase was isolated and sequenced. CAC1 is a single-copy gene interrupted by six introns. Subcellular immunogold labeling indicates that the biotin carboxyl-carrier
An embryo-lethal mutant of Arabidopsis thaliana is a biotin auxotroph.
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Lethal mutants have been used in a variety of animal systems to study the genetic control of morphogenesis and differentiation. Abnormal development has been shown in some cases to be caused by defects in basic cellular processes. We describe in this report an embryo-lethal mutant of Arabidopsis
Biochemical and molecular biological characterization of CAC2, the Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the plastidic acetyl-coenzyme A carboxylase.
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The biotin carboxylase subunit of the heteromeric chloroplastic acetyl-coenzyme A carboxylase (ACCase) of Arabidopsis thaliana is coded by a single gene (CAC2), which is interrupted by 15 introns. The cDNA encodes a deduced protein of 537 amino acids with an apparent N-terminal chloroplast-targeting
Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase domains of acetyl-CoA carboxylase: assignment of the domain structure in a full-length Arabidopsis thaliana genomic clone.
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One independent and two overlapping rape cDNA clones have been isolated from a rape embryo library. We have shown that they encode a 2.3 kb and a 2.5 kb stretch of the full-length acetyl-CoA carboxylase (ACCase) cDNA, corresponding to the biotin-binding and transcarboxylase domains respectively.
Biotin synthesis in higher plants: isolation of a cDNA encoding Arabidopsis thaliana bioB-gene product equivalent by functional complementation of a biotin auxotroph mutant bioB105 of Escherichia coli K12.
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Biotin synthase is involved in the conversion of dethiobiotin to biotin in bacteria, yeast and higher plants. We isolated a complete cDNA (1.3 kb) encoding A. thaliana bioB-gene product by functional complementation of the bioB105 biotin auxotroph mutant of Escherichia coli K12 using an A. thaliana
Assembly of a gene sequence tag microarray by reversible biotin-streptavidin capture for transcript analysis of Arabidopsis thaliana.
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BACKGROUND
Transcriptional profiling using microarrays has developed into a key molecular tool for the elucidation of gene function and gene regulation. Microarray platforms based on either oligonucleotides or purified amplification products have been utilised in parallel to produce large amounts of
Both antisense and sense expression of biotin carboxyl carrier protein isoform 2 inactivates the plastid acetyl-coenzyme A carboxylase in Arabidopsis thaliana.
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To further characterize the role of biotin carboxyl carrier protein isoform 2 (BCCP2) in acetyl-coenzyme A carboxylase (ACCase) function and fatty acid biosynthesis, plants with reduced or increased expression of this protein were characterized. Analysis of 38 independent Arabidopsis lines
A newly discovered function of peroxisomes: involvement in biotin biosynthesis.
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In plants, peroxisomes are the organelles involved in various metabolic processes and physiological functions including β-oxidation, mobilization of seed storage lipids, photorespiration, and hormone biosynthesis. We have recently shown that, in fungi and plants, peroxisomes play a vital role in
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