ArticleThe Plant cell2001
IAA17/AXR3: biochemical insight into an auxin mutant phenotype.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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Who cites it
118 citing papers in PubMed.
- Light and Shadows: Insights from Large-Scale Visual Screens for Arabidopsis Leaf Morphology Mutants.International journal of molecular sciences · 2025Review
- Core biological principles and tools stemming from basic Arabidopsis research.The Plant cell · 2025Review
- Dressed Up to the Nines: The Interplay of Phytohormones Signaling and Redox Metabolism During Plant Response to Drought.Plants (Basel, Switzerland) · 2025Review
- Genome-Wide Identification and Characterization of thePlants (Basel, Switzerland) · 2024Article
- Overexpression of Auxin/Indole-3-Acetic Acid Gene TrIAA27 Enhances Biomass, Drought, and Salt Tolerance inPlants (Basel, Switzerland) · 2024Article
- Genome-Wide Identification and Analysis of the Aux/IAA Gene Family inInternational journal of molecular sciences · 2024Article
- To bind or not to bind: how AUXIN RESPONSE FACTORs select their target genes.Journal of experimental botany · 2023Review
- Analysis of Auxin-Encoding Gene Family inPlants (Basel, Switzerland) · 2023Article
- Unraveling the Guardians of Growth: A Comprehensive Analysis of thePlants (Basel, Switzerland) · 2023Article
- Transcriptome Sequencing Analysis of Root in Soybean Responding to Mn Poisoning.International journal of molecular sciences · 2023Article
- Genome-wide identification and expression analysis of the AUX/IAA gene family in turnip (Brassica rapa ssp. rapa).BMC plant biology · 2023Article
- Article
- SUMO E3 ligase AtMMS21-dependent SUMOylation of AUXIN/INDOLE-3-ACETIC ACID 17 regulates auxin signaling.Plant physiology · 2023Article
- Cooperative action of separate interaction domains promotes high-affinity DNA binding ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Relative Protein Lifetime Measurement in Plants Using Tandem Fluorescent Protein Timers.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Rice EIL1 interacts with OsIAAs to regulate auxin biosynthesis mediated by the tryptophan aminotransferase MHZ10/OsTAR2 during root ethylene responses.The Plant cell · 2022Article
- Structural Aspects of Auxin Signaling.Cold Spring Harbor perspectives in biology · 2022Review
- Genome-wide identification of Aux/IAA gene family and their expression analysis inFrontiers in genetics · 2022Article
- Genome-wide characterization and expression analyses of the auxin/indole-3-acetic acid (Aux/IAA) gene family in barley (Hordeum vulgare L.).Scientific reports · 2020Article
- Different knockout genotypes of OsIAA23 in rice using CRISPR/Cas9 generating different phenotypes.Plant molecular biology · 2019Article
58 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
The Aux/IAA genes are rapidly and specifically induced by the plant hormone auxin. The proteins encoded by this gene family are short-lived nuclear proteins that are capable of homodimerizing and heterodimerizing. Molecular, biochemical, and genetic data suggest that these proteins are involved in auxin signaling. The pleiotropic morphological phenotype and altered auxin responses of the semidominant axr3-1 mutant of Arabidopsis result from a single amino acid change in the conserved domain II of the Aux/IAA protein IAA17. Here, we show that the biochemical effect of this gain-of-function mutation is to increase the half-life of the iaa17/axr3-1 protein by sevenfold. Intragenic mutations that suppress the iaa17/axr3-1 phenotype have been described. The iaa17/axr3-1R3 revertant contains a second site mutation in domain I and the iaa17/axr3-1R2 revertant contains a second site mutation in domain III. Transient expression assays show that the mutant forms of IAA17/AXR3 retain the ability to accumulate in the nucleus. Using the yeast two hybrid system, we show that the iaa17/axr3-1 mutation does not affect homodimerization. However, the iaa17/axr3-1 revertants counteract the increased levels of iaa17/axr3-1 protein by decreasing the capacity of the mutant protein to homodimerize. Interestingly, heterodimerization of the revertant forms of IAA17/AXR3 with IAA3/SHY2, another Aux/IAA protein, and ARF1 or ARF5/MP proteins is affected only by changes in domain III. Collectively, the results provide biochemical evidence that the revertant mutations in the IAA17/AXR3 gene affect the capacity of the encoded protein to dimerize with itself, other members of the Aux/IAA protein family, and members of the ARF protein family. By extension, these findings may provide insight into the effects of analogous mutations in other members of the Aux/IAA gene family.
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