
doi: 10.1038/35104500
pmid: 11713520
The plant hormone auxin is central in many aspects of plant development. Previous studies have implicated the ubiquitin-ligase SCF(TIR1) and the AUX/IAA proteins in auxin response. Dominant mutations in several AUX/IAA genes confer pleiotropic auxin-related phenotypes, whereas recessive mutations affecting the function of SCF(TIR1) decrease auxin response. Here we show that SCF(TIR1) is required for AUX/IAA degradation. We demonstrate that SCF(TIR1) interacts with AXR2/IAA7 and AXR3/IAA17, and that domain II of these proteins is necessary and sufficient for this interaction. Further, auxin stimulates binding of SCF(TIR1) to the AUX/IAA proteins, and their degradation. Because domain II is conserved in nearly all AUX/IAA proteins in Arabidopsis, we propose that auxin promotes the degradation of this large family of transcriptional regulators, leading to diverse downstream effects.
SKP Cullin F-Box Protein Ligases, Indoleacetic Acids, Arabidopsis Proteins, Ubiquitin, Recombinant Fusion Proteins, Amino Acid Motifs, Arabidopsis, Nuclear Proteins, Plants, Genetically Modified, Gene Expression Regulation, Plant, Mutation, Peptide Synthases, Growth Substances, Glucuronidase, Plant Proteins, Protein Binding, Transcription Factors
SKP Cullin F-Box Protein Ligases, Indoleacetic Acids, Arabidopsis Proteins, Ubiquitin, Recombinant Fusion Proteins, Amino Acid Motifs, Arabidopsis, Nuclear Proteins, Plants, Genetically Modified, Gene Expression Regulation, Plant, Mutation, Peptide Synthases, Growth Substances, Glucuronidase, Plant Proteins, Protein Binding, Transcription Factors
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