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Intrinsic disorder and conformational co-existence in auxin co-receptors
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Ramans-Harborough, Sigurd, Kalverda, Arnout P. , Manfield, Iain W., Thompson, Gary S., Kieffer, Martin, Uzunova, Veselina, Quareshy, Mussa, Prusinska, Justyna M., Roychoudhry, Suruchi, Hayashi, Ken-ichiro, Napier, Richard, del Genio, Charo and Kepinski, Stefan (2023) Intrinsic disorder and conformational co-existence in auxin co-receptors. Proceedings of the National Academy of Sciences, 120 (40). e2221286120. doi:10.1073/pnas.2221286120 ISSN 0027-8424.
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Official URL: https://doi.org/10.1073/pnas.2221286120
Abstract
AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) transcriptional repressor proteins and the TRANSPORT INHIBITOR RESISTANT 1/AUXIN SIGNALING F-BOX (TIR1/AFB) proteins to which they bind act as auxin coreceptors. While the structure of TIR1 has been solved, structural characterization of the regions of the Aux/IAA protein responsible for auxin perception has been complicated by their predicted disorder. Here, we use NMR, CD and molecular dynamics simulation to investigate the N-terminal domains of the Aux/IAA protein IAA17/AXR3. We show that despite the conformational flexibility of the region, a critical W–P bond in the core of the Aux/IAA degron motif occurs at a strikingly high (1:1) ratio of cis to trans isomers, consistent with the requirement of the cis conformer for the formation of the fully-docked receptor complex. We show that the N-terminal half of AXR3 is a mixture of multiple transiently structured conformations with a propensity for two predominant and distinct conformational subpopulations within the overall ensemble. These two states were modeled together with the C-terminal PB1 domain to provide the first complete simulation of an Aux/IAA. Using MD to recreate the assembly of each complex in the presence of auxin, both structural arrangements were shown to engage with the TIR1 receptor, and contact maps from the simulations match closely observations of NMR signal-decreases. Together, our results and approach provide a platform for exploring the functional significance of variation in the Aux/IAA coreceptor family and for understanding the role of intrinsic disorder in auxin signal transduction and other signaling systems.
Item Type: | Journal Article | ||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
Journal or Publication Title: | Proceedings of the National Academy of Sciences | ||||||
Publisher: | National Academy of Sciences | ||||||
ISSN: | 0027-8424 | ||||||
Official Date: | 27 September 2023 | ||||||
Dates: |
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Volume: | 120 | ||||||
Number: | 40 | ||||||
Article Number: | e2221286120 | ||||||
DOI: | 10.1073/pnas.2221286120 | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||
Date of first compliant deposit: | 23 August 2023 | ||||||
Date of first compliant Open Access: | 29 September 2023 | ||||||
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