Biotin Synthase from Arabidopsis thaliana (cDNA Isolation and Characterization of Gene Expression)

Patton, David A.; Johnson, Marie; Ward, Eric

doi:10.1104/pp.112.1.371

Cited by 33 publications

(22 citation statements)

References 26 publications

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“…In Arabidopsis, a biotin limiting condition was able to induce 5-fold increase in bio2 expression. They also showed that the expression of bio2 changes during the light/dark cycle and that the trend is reproducible and consistent with the regulation by light or circadian rhythms (16). Previously, we observed that the biotin content in vegetables in Japan is dependent on the climate conditions of the cultivation area (22).…”

supporting

confidence: 74%

“…This step includes reactions that form a thiophene ring via the addition of a sulfur atom and is considered to be a rate-limiting step for biotin synthesis (21). In Arabidopsis, the expression of bio2 is reportedly regulated in response to development, light, the circadian period, and biotin starvation (16). Accordingly, the expression status of bio2 in the sprouts of each group was determined by quantitating the transcripts with real-time PCR.…”

Section: Expression Of the Bio2 Gene In Pea Sprouts Is Suppressed Undmentioning

confidence: 99%

“…The second and third steps are catalyzed by a bifunctional fusion protein comprised of DAPA synthase (Bio1) and DTB synthase (Bio3), which produce DTB in the mitochondria (15). The final step, conversion of DTB to biotin, occurs in the mitochondria with a stepwise reaction catalyzed by biotin synthase (Bio2) (14,16), which then forms the thiophane ring of biotin through the oxidative addition of a sulfur atom between the C6 methylene and C9 methyl groups of DTB (17). Bio2 is a member of the radical S-adenosyl-l-methionine (SAM) superfamily of enzymes that interact with iron-sulfur clusters and convert SAM to methionine and a highly reactive 5′-deoxyadenosyl radical, which is used to form the C-S bonds in biotin.…”

mentioning

confidence: 99%

“…Patton et al reported that the expression of the plant biotin synthase gene (bio2) is regulated by the cellular concentration of biotin (16). In Arabidopsis, a biotin limiting condition was able to induce 5-fold increase in bio2 expression.…”

mentioning

confidence: 99%

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The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

Kamiyama

Ohnuki

Moriki

et al. 2016

J Nutr Sci Vitaminol

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Summary Biotin is an essential micronutrient, and is a cofactor for several carboxylases that are involved in the metabolism of glucose, fatty acids, and amino acids. Because plant cells can synthesize their own biotin, a wide variety of plant-based foods contains significant amounts of biotin; however, the influence of environmental conditions on the biotin content in plants remains largely unclear. In the present study, we investigated the effects of different cultivation conditions on the biotin content and biotin synthesis in pea sprouts (Pisum sativum Compared to the biotin content of pea sprouts under the control conditions, the biotin contents of pea sprouts under the low-light, dark, and cold conditions had significantly decreased. The dark group showed the lowest biotin content among the groups. Expression of the biotin synthase gene (bio2) was also significantly decreased under the dark and cold conditions compared to the control condition, in a manner similar to that observed for the biotin content. No significant differences in the adenosine triphosphate content were observed among the groups. These results indicate that environmental conditions such as light and temperature modulate the biotin content of pea plant tissues by regulating the expression of biotin synthase.

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supporting

confidence: 74%

Section: Expression Of the Bio2 Gene In Pea Sprouts Is Suppressed Undmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

Kamiyama

Ohnuki

Moriki

et al. 2016

J Nutr Sci Vitaminol

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“…Two conserved C motifs, C-E-E-A-X-C-P-N-X-X-E-C and C-T-R-X-C-X-F-C, were found at positions from 103 to 114 and 135 to 142 in the Arabidopsis LIP1 protein, respectively. The second C motif is also conserved in biotin synthases of Arabidopsis (Patton et al, 1996;Weaver et al, 1996) and microorganisms (Otsuka et al, 1988;Zhang et al, 1994;Bower et al, 1996). Since lipoic acid synthase and biotin synthase catalyze a similar reaction that inserts a sulfur atom into a hydrocarbon chain, the conserved C residues may play an important role in this process.…”

Section: Identification Of the Cdna Coding For Arabidopsis Lipoic Acimentioning

confidence: 99%

Biosynthesis of Lipoic Acid in Arabidopsis: Cloning and Characterization of the cDNA for Lipoic Acid Synthase

Yasuno

Wada

1998

Plant Physiology

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Lipoic acid is a coenzyme that is essential for the activity of enzyme complexes such as those of pyruvate dehydrogenase and glycine decarboxylase. We report here the isolation and characterization of LIP1 cDNA for lipoic acid synthase of Arabidopsis. The Arabidopsis LIP1 cDNA was isolated using an expressed sequence tag homologous to the lipoic acid synthase of Escherichia coli. This cDNA was shown to code for Arabidopsis lipoic acid synthase by its ability to complement a lipA mutant of E. coli defective in lipoic acid synthase. DNA-sequence analysis of the LIP1 cDNA revealed an open reading frame predicting a protein of 374 amino acids. Comparisons of the deduced amino acid sequence with those of E. coli and yeast lipoic acid synthase homologs showed a high degree of sequence similarity and the presence of a leader sequence presumably required for import into the mitochondria. Southernhybridization analysis suggested that LIP1 is a single-copy gene in Arabidopsis. Western analysis with an antibody against lipoic acid synthase demonstrated that this enzyme is located in the mitochondrial compartment in Arabidopsis cells as a 43-kD polypeptide.Lipoic acid (6,8-thioctic acid) is a sulfur-containing coenzyme that is required for the activity of enzyme complexes involved in the oxidative decarboxylation of ␣-ketoacids (Reed and Hackert, 1990;Perham, 1991;Mattevi et al., 1992) and in the Gly-cleavage system (Fujiwara et al., 1990;Kim and Oliver, 1990;Macherel et al., 1990). There are five lipoyl proteins: the dihydrolipoamide acyltransferase subunits of pyruvate, ␣-ketoglutarate, branched-chain ␣-ketoacid dehydrogenase complexes, protein X of the pyruvate dehydrogenase complex, and the H-protein of the Gly-cleavage system. Lipoic acid is covalently bound to these proteins via an amide linkage to the ⑀-amino group of specific Lys residues (Reed and Hackert, 1966). The lipoylLys arm functions as a carrier of reaction intermediates, and reducing equivalents interact with the active sites of the components of the complexes (Yeaman, 1989; Douce et al., 1994).Despite the importance of the lipoyl-prosthetic group in the functioning of several enzyme complexes, the biosynthesis of lipoic acid is not well understood in any organism. Molecular genetic studies (Vanden Boom et al., 1991;Reed and Cronan, 1993;Morris et al., 1994Morris et al., , 1995 of Escherichia coli have identified three genes, lipA, lipB, and lplA that are involved in the biosynthesis and transfer of lipoic acid. lipA encodes a lipoic acid synthase that is required for an insertion of the first sulfur atom into the octanoate backbone (Reed and Cronan, 1993). lplA and lipB encode lipoate ligases that are involved in the transfer of lipoic acid to cognate proteins (Morris et al., 1994(Morris et al., , 1995. LplA and LipB proteins primarily function in the utilization of lipoic acid exogenously added to the growth medium and endogenously synthesized lipoic acid in E. coli cells, respectively (Morris et al., 1994(Morris et al., , 1995. LplA protein is involved...

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The design and synthesis of inhibitors of dethiobiotin synthetase as potential herbicides

et al. 1999

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Dethiobiotin synthetase (DTBS ; E.C. 6.6.6.6), the penultimate enzyme in the biosynthesis of the essential vitamin biotin, is a new potential target for novel herbicides. Inhibitors were designed based on mechanistic and structural information. The in-vitro activities of these potential inhibitors versus the bacterial enzyme are reported here. Mimics of 7,8-diaminopelargonic acid (DAPA) or the DAPA carbamate reaction intermediate were substrates or partial substrates for the enzyme. Synergistic binding with ATP was noted with compounds which contained an amino functionality. NMR studies and X-ray structures conürmed that the inhibitors could be phosphorylated by the enzyme. Several series of potential inhibitors were designed to take advantage of this partial substrate activity by generating potentially more tightly bound phosphorylated inhibitors in situ. Structure-activity relationships for these series based on both substrate and inhibitory activity are described herein. An X-ray structure for one of these inhibitors is also discussed. Although considerable potential for inhibitors of this type was demonstrated, none of the compounds reported showed sufficient herbicidal activity to be a commercial proposition.

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Biotin Synthase from Arabidopsis thaliana (cDNA Isolation and Characterization of Gene Expression)

Cited by 33 publications

References 26 publications

The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

Biosynthesis of Lipoic Acid in Arabidopsis: Cloning and Characterization of the cDNA for Lipoic Acid Synthase

The design and synthesis of inhibitors of dethiobiotin synthetase as potential herbicides

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