2.オーキシン受容体TIR1に特異的な新規オーキシンプローブの作用機構(口頭発表)

概要

論文の詳細を見る
We developed alpha-alkyl-auxin as a novel auxin probe to specifically modulate TIR1 function, an auxin receptor. TIR1 is F-Box protein, a component of an SCF-class E3 ubiquitin-ligase. To reveal the molecular mechanism of auxin probes, we solved crystal structure of three complexes of TIR1-ASK1-probe (an agonist or two antagonists). Crystal structure of three complexes revealed the probes bind to an auxin-binding site of TIR1 and modulate the TIR1 recognition process for Aux/IAA represser. Furthermore, no conformational change of TIR1 was observed among the three complexes. Additionally, molecular docking calculation between TIR1 and probe also support the molecular mechanism of probe action. These evidences clearly indicate that auxin actually works as 'a molecular glue'in TIR1 complex proposed by a recent study. This is the first report on a molecular mechanistic study for anti-auxin probe and a modulator of the substrate recognition in SCF-class ubiquitin-ligase complex.
植物化学調節学会の論文
2007-10-05