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hyoscyamus muticus/nicotina
L'enllaç es desa al porta-retalls
13 resultats
Hyoscyamus muticus + Nicotiana tabacum fusion hybrids selected via auxotroph complementation.
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Protoplasts of the nicotinamide-deficient Hyoscyamus muticus cell line nic(-) IVH2 and of the nitrate reductase-deficient Nicotiana tabacum cell line NR(-) cnx 68 were induced to fuse. Selection for putative interspecific hybrid clones was via auxotroph complementation. Controls included tests for
A soluble auxin-binding protein from Hyoscyamus muticus is a glutathione S-transferase.
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We have used the photoaffinity label azido-[3H]IAA (5-N3-[7-3H]indole-3-acetic acid), a biologically active analog of indole-3-acetic acid, to identify auxin-binding proteins (ABPs) in the soluble fraction of Hyoscyamus muticus. A 25-kD polypeptide previously described (H. Macdonald, A. M. Jones, P.
Biotransformation of hyoscyamine into scopolamine in transgenic tobacco cell cultures.
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Hyoscyamine-6beta-hydroxylase (H6H) catalyses the conversion of hyoscyamine into its epoxide scopolamine, a compound with a higher added value in the pharmaceutical market than hyoscyamine. We report the establishment of tobacco cell cultures carrying the Hyoscyamus muticus h6h gene under the
Cloning and bacterial expression of a sesquiterpene cyclase from Hyoscyamus muticus and its molecular comparison to related terpene cyclases.
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Genomic and cDNA clones for vetispiradiene synthase, a sesquiterpene cyclase found in Hyoscyamus muticus, were isolated using a combination of reverse transcription-polymerase chain reactions and conventional cloning procedures. RNA blot hybridization demonstrated an induction of mRNA consistent
Enhanced secretion of tropane alkaloids in Nicotiana tabacum hairy roots expressing heterologous hyoscyamine-6beta-hydroxylase.
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Hyoscyamine-6beta-hydroxylase (H6H; EC 1.14.11.11) catalyses oxidative reactions in the biosynthetic pathway leading from hyoscyamine to the more pharmaceutically valuable tropane alkaloid scopolamine. The h6h gene encoding H6H from Hyoscyamus niger was introduced, under the control of the CaMV 35S
Effect of pmt gene overexpression on tropane alkaloid production in transformed root cultures of Datura metel and Hyoscyamus muticus.
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In order to increase the production of the pharmaceuticals hyoscyamine and scopolamine in hairy root cultures, a binary vector system was developed to introduce the T-DNA of the Ri plasmid together with the tobacco pmt gene under the control of CaMV 35S promoter, into the genome of Datura metel and
Reconstitution of plant nitrate reductase by Escherichia coli extracts and the molecular cloning of the chlA gene of Escherichia coli K12.
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Extracts from Escherichia coli, wild type and chlB, chlC, chlD, chlE, and chlG, but not chlA mutants, were able to reconstitute the nitrate reductase activity in Nicotiana tabacum cnx68 and Hyoscyamus muticus MA-2 mutant extracts. Because cnx68 and MA-2 lack the molybdenum cofactor required for
Agarose plating and a bead type culture technique enable and stimulate development of protoplast-derived colonies in a number of plant species.
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Two novel techniques improve division and colony formation from protoplasts: 1) Plating in agarose stimulates colony formation of protoplasts from a wide range of species. Protoplasts from Nicotiana tabacum developed to colonies from lower initial population densities in agarose than in agar or
Species-specific repetitive DNA used to identify interspecific somatic hybrids.
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Plasmid DNA clones containing repetitive DNA sequences were isolated from Hyoscyamus muticus and Nicotiana tabacum. Non cross-hybridizing probes from each species were used in a simple hybridization test with DNA isolated from presumptive somatic hybrids. This allowed unequivocal identification of
X-ray irradiation promoted asymmetric somatic hybridisation and molecular analysis of the products.
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Complementation of two metabolic deficiences - nitrate reductase and tryptophan synthase - was used to select for somatic fusion hybrids between tobacco (Nicotiana tabacum) and henbane (Hyoscyamus muticus) with prior X-irradiation of one partner. Using species specific, radioactively labelled DNA
Quantitative exploration of the catalytic landscape separating divergent plant sesquiterpene synthases.
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Throughout molecular evolution, organisms create assorted chemicals in response to varying ecological niches. Catalytic landscapes underlie metabolic evolution, wherein mutational steps alter the biosynthetic properties of enzymes. Here we report the first systematic quantitative characterization of
Identifying functional domains within terpene cyclases using a domain-swapping strategy.
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Cyclic terpenes and terpenoids are found throughout nature. They comprise an especially important class of compounds from plants that mediate plant- environment interactions, and they serve as pharmaceutical agents with antimicrobial and anti-tumor activities. Molecular comparisons of several
Biosynthetic potential of sesquiterpene synthases: product profiles of Egyptian Henbane premnaspirodiene synthase and related mutants.
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The plant terpene synthase (TPS) family is responsible for the biosynthesis of a variety of terpenoid natural products possessing diverse biological functions. TPSs catalyze the ionization and, most commonly, rearrangement and cyclization of prenyl diphosphate substrates, forming linear and cyclic
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