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Agrobacterium T‐DNA gene 1 codes for tryptophan 2‐monooxygenase activity in tobacco crown gall cells
Author(s) -
Van Onckelen H.,
Prinsen E.,
Inzé D.,
Rüdeisheim P.,
Van Lijsebettens M.,
Follin A.,
Schell J.,
Van Montagu M.,
De Greef J.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80436-7
Subject(s) - agrobacterium tumefaciens , mutant , biology , agrobacterium , gene , tryptophan , dna , gall , microbiology and biotechnology , biochemistry , ti plasmid , nicotiana tabacum , monooxygenase , transformation (genetics) , amino acid , enzyme , botany , cytochrome p450
Cloned tobacco crown gall tissue induced by the Agrobacterium tumefaciens C58 T‐DNA mutant pGV3132, defective for the T‐DNA‐encoded amihydrolase ( iaa H), accumulates about 1000‐times more indole‐3‐acet‐amide (IAM) when compared to untransformed tobacco callus and crown gall tissue induced by a T‐DNA mutant defective for gene 1 . In vitro experiments demonstrated that this IAM accumulation is correlated with the active conversion of Trp into IAM. The results presented in this report provide biochemical evidence that the T‐DNA gene 1 encodes a tryptophan 2‐monooxygenase ( iaa M) activity in transformed plant cells. This gene cooperates with the gene 2‐encoded amidohydrolase ( iaa H) in the T‐DNA‐controlled indole‐3‐acetic acid (IAA) biosynthesis pathway in crown gall cells.