The Pseudomonas savastanoi tryptophan-2-mono-oxygenase is biologically active in Nicotiana tabacum |
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Authors: | D Inzé A Follin J Velten L Velten E Prinsen P Rüdelsheim H Van Onckelen J Schell M Van Montagu |
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Institution: | (1) Laboratorium voor Genetica, Rijksuniversiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium;(2) Max-Planck-Institut für Züchtungsforschung, D-5000 Köln, FRG;(3) Department Biologie, Universitaire Instelling Antwerpen, B-2610 Antwerpen, Belgium;(4) Present address: Department of Chemistry, New Mexico State University, 88003 Las Cruces, N.M., USA |
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Abstract: | It has been proposed that the eukaryotic T-DNA-encoded indole-3-acetic acid (IAA) biosynthesis genes of Agrobacterium tumefaciens and their prokaryotic counterpart in Pseudomonas savastanoi originated from common ancestor genes. This paper provides additional evidence for the functional similarity between the gene products. We have demonstrated that a chimeric gene consisting of the coding sequence of the P. savastanoi tryptophan-2-mono-oxygenase (iaaM gene) and a plant promoter encodes an active enzyme in Nicotiana tabacum. Transformants obtained with this chimeric gene grew as a callus on hormone-free media. No stably transformed plantlets could be isolated. The callus tissues contained extremely high levels of indole-3-acetamide and slightly elevated levels of IAA. Either indole-3-acetamide by itself has a low auxin activity or, alternatively, it is converted aspecifically and at low rates into IAA. The P. savastanoi tryptophan-2-mono-oxygenase activity in plants is also able to detoxify the amino-acid analogue 5-methyltryptophan. This property can be used for positive selection of transformed calli.Abbreviations BAP
6-benzylaminopurine
- IAA
indole-3-acetic acid
- IAM
indole-3-acetamide
- NAA
naphthalene-1-acetic acid
- NPT-II
neomycin phosphotransferase II
- T-DNA
transferred DNA |
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Keywords: | Agrobacterium Auxin biosynthesis Indole-3-acetamide Pseudomonas Tryptophan-2-mono-oxygenase |
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