Latest Publications
Intrinsic disorder and conformational co-existence in auxin co-receptors
Sigurd Ramans-Harborough, Arnout P. Kalverda, Iain W. Manfield, Gary S. Thompson, Martin Kieffer, Veselina Uzunova, Mussa Quareshy, Justyna M. Prusinska, Suruchi Roychoudhry, Ken-ichiro Hayashi, Richard Napier, Charo del Genio, Stefan Kepinski
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. 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.