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PMID: 11805067 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Arabidopsis cytochrome P450 cyp83B1 mutations activate the tryptophan biosynthetic pathway.

Genetics ·Vol. 160 ·No. 1 ·2002-01-00 ·Pages 323-32

Smolen G, Bender J

Abstract

In plants, the tryptophan biosynthetic pathway provides a number of important secondary metabolites including the growth regulator indole-3-acetic acid (IAA) and indole glucosinolate defense compounds. Genes encoding tryptophan pathway enzymes are transcriptionally induced by a variety of stress signals, presumably to increase the production of both tryptophan and secondary metabolites during defense responses. To understand the mechanism of transcriptional induction, we isolated altered tryptophan regulation (atr) mutants in Arabidopsis thaliana with activated transcription of tryptophan genes. One atr complementation group consisted of mutations in the cytochrome P450 gene CYP83B1. Mutant plants had constitutively activated expression of the ATR1 Myb factor gene, which was identified as a positive regulator of tryptophan genes via the atr mutant screen. cyp83B1 mutants were previously characterized as having defects in IAA homeostasis due to perturbation of secondary tryptophan metabolism. Our findings indicate that the upregulation of tryptophan pathway genes might also contribute to the overaccumulation of IAA in mutant plants. Moreover, we show that cyp83B1 mutants have lesion-mimic phenotypes, suggesting that multiple stress pathways are activated by loss of CYP83B1 function.

MeSH Terms
Arabidopsis/enzymology,genetics,metabolism Arabidopsis Proteins Cloning, Molecular Cytochrome P-450 Enzyme System/genetics,physiology Gene Expression Regulation, Plant/genetics,physiology Mixed Function Oxygenases/physiology Mutation Oxygenases/genetics Tryptophan/biosynthesis,genetics Up-Regulation
Chemicals
Arabidopsis Proteins Tryptophan Cytochrome P-450 Enzyme System Mixed Function Oxygenases Oxygenases CYP83B1 protein, Arabidopsis salicylate 1-monooxygenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Smolen Gromoslaw
Department of Biochemistry and Molecular Biology, Johns Hopkins University, Bloomberg School of Public Health, Baltimore, Maryland 21205, USA.
Bender Judith
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Article Info
Journal
Genetics
Abbr.
Genetics
ISSN
0016-6731
Published
2002-01-00
Pages
323-32
Language
English
Region
United States
NLM ID
0374636
PMCID
PMC1461936
Subset
IM
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