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Originally published as Genetics Published Articles Ahead of Print on August 24, 2008.
Genetics, Vol. 180, 237-251, September 2008, Copyright © 2008
doi:10.1534/genetics.108.090399
Identification and Characterization of Arabidopsis Indole-3-Butyric Acid Response Mutants Defective in Novel Peroxisomal Enzymes
Bethany K. Zolman*,1,
Naxhiely Martinez
,
Arthur Millius,2,
A. Raquel Adham and
Bonnie Bartel
* Department of Biology, University of Missouri, St. Louis, Missouri 63121 and Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005
1 Corresponding author: Department of Biology, University of Missouri, R223 Research Bldg., 1 University Blvd., St. Louis, MO 63121-4400.
E-mail: zolmanb{at}umsl.edu
Genetic evidence suggests that indole-3-butyric acid (IBA) is converted to the active auxin indole-3-acetic acid (IAA) by removal of two side-chain methylene units in a process similar to fatty acid β-oxidation. Previous studies implicate peroxisomes as the site of IBA metabolism, although the enzymes that act in this process are still being identified. Here, we describe two IBA-response mutants, ibr1 and ibr10. Like the previously described ibr3 mutant, which disrupts a putative peroxisomal acyl-CoA oxidase/dehydrogenase, ibr1 and ibr10 display normal IAA responses and defective IBA responses. These defects include reduced root elongation inhibition, decreased lateral root initiation, and reduced IBA-responsive gene expression. However, peroxisomal energy-generating pathways necessary during early seedling development are unaffected in the mutants. Positional cloning of the genes responsible for the mutant defects reveals that IBR1 encodes a member of the short-chain dehydrogenase/reductase family and that IBR10 resembles enoyl-CoA hydratases/isomerases. Both enzymes contain C-terminal peroxisomal-targeting signals, consistent with IBA metabolism occurring in peroxisomes. We present a model in which IBR3, IBR10, and IBR1 may act sequentially in peroxisomal IBA β-oxidation to IAA.
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