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PMID: 15743450 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation.

The Plant journal : for cell and molecular biology ·Vol. 41 ·No. 6 ·2005-03-00 ·Pages 859-74

Adham AR, Zolman BK, Millius A, Bartel B

Abstract

Indole-3-butyric acid (IBA) is an endogenous auxin used to enhance rooting during propagation. To better understand the role of IBA, we isolated Arabidopsis IBA-response (ibr) mutants that display enhanced root elongation on inhibitory IBA concentrations but maintain wild-type responses to indole-3-acetic acid, the principle active auxin. A subset of ibr mutants remains sensitive to the stimulatory effects of IBA on lateral root initiation. These mutants are not sucrose dependent during early seedling development, indicating that peroxisomal beta-oxidation of seed storage fatty acids is occurring. We used positional cloning to determine that one mutant is defective in ACX1 and two are defective in ACX3, two of the six Arabidopsis fatty acyl-CoA oxidase (ACX) genes. Characterization of T-DNA insertion mutants defective in the other ACX genes revealed reduced IBA responses in a third gene, ACX4. Activity assays demonstrated that mutants defective in ACX1, ACX3, or ACX4 have reduced fatty acyl-CoA oxidase activity on specific substrates. Moreover, acx1 acx2 double mutants display enhanced IBA resistance and are sucrose dependent during seedling development, whereas acx1 acx3 and acx1 acx5 double mutants display enhanced IBA resistance but remain sucrose independent. The inability of ACX1, ACX3, and ACX4 to fully compensate for one another in IBA-mediated root elongation inhibition and the ability of ACX2 and ACX5 to contribute to IBA response suggests that IBA-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and IBA beta-oxidation, rather than direct enzymatic activity of ACX isozymes on IBA-CoA.

MeSH Terms
Acyl-CoA Oxidase/genetics,metabolism Amino Acid Sequence Arabidopsis/enzymology,genetics Gene Expression Indoleacetic Acids/metabolism Indoles/metabolism Molecular Sequence Data Mutation Oxidation-Reduction Phenotype Phylogeny Sequence Alignment
Chemicals
Indoleacetic Acids Indoles indolebutyric acid Acyl-CoA Oxidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Adham A Raquel
Department of Biochemistry and Cell Biology, Rice University, MS-140, Houston, TX 77005, USA.
Zolman Bethany K
Millius Arthur
Bartel Bonnie
Article Info
Journal
The Plant journal : for cell and molecular biology
Abbr.
Plant J
ISSN
0960-7412
Published
2005-03-00
Pages
859-74
Language
English
Region
England
NLM ID
9207397
Subset
IM
Grants
NIGMS NIH HHS · F31-GM066373 · United States
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