Journal
NATURE CHEMICAL BIOLOGY
Volume 8, Issue 5, Pages 477-485Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.926
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Funding
- US National Institutes of Health (NIH) [R01 CA107134, T32 GM07270]
- HHMI
- UK Biotechnology and Biological Sciences Research Council [BB/F013981/1, BB/F014651/1]
- NIH
- US National Science Foundation
- BBSRC [BB/F013981/1, BB/F014651/1, BB/F007418/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F007418/1, BB/F014651/1, BB/F013981/1] Funding Source: researchfish
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The plant hormone auxin regulates virtually every aspect of plant growth and development. Auxin acts by binding the F-box protein transport inhibitor response 1 (TIR1) and promotes the degradation of the AUXIN/INDOLE-3-ACETIC ACID (Aux/IAA) transcriptional repressors. Here we show that efficient auxin binding requires assembly of an auxin co-receptor complex consisting of TIR1 and an Aux/IAA protein. Heterologous experiments in yeast and quantitative IAA binding assays using purified proteins showed that different combinations of TIR1 and Aux/IAA proteins form co-receptor complexes with a wide range of auxin-binding affinities. Auxin affinity seems to be largely determined by the Aux/IAA. As there are 6 TIR1/AUXIN SIGNALING F-BOX proteins (AFBs) and 29 Aux/IAA proteins in Arabidopsis thaliana, combinatorial interactions may result in many co-receptors with distinct auxin-sensing properties. We also demonstrate that the AFB5-Aux/IAA co-receptor selectively binds the auxinic herbicide picloram. This co-receptor system broadens the effective concentration range of the hormone and may contribute to the complexity of auxin response.
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