Structural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling.

Structural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling.
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DOI:
10.1038/s41586-018-0743-5
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发表时间:
2018-11
期刊:
影响因子:
64.8
通讯作者:
Zheng N
Zheng N
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Shabek N;Ticchiarelli F;Mao H;Hinds TR;Leyser O;Zheng N

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植物激素独脚金内酯(SL)调节植物生理的许多方面。在芽分支抑制中,SL代谢α/β水解酶D14与F-box蛋白D3相互作用,泛素化并降解转录阻遏物D53。尽管最近确定了D14-SL相互作用的多种模式,但水解酶如何与D3一起介导D53泛素化仍然是难以捉摸的。在这里,我们发现D3具有C-末端α-螺旋(CTH),可以在两种构象状态之间切换。与其促进D3和D14与水解的SL中间体结合的接合形式不同,移位的D3 CTH可以识别开放构象的未修饰的D14并抑制其酶活性。以SL依赖性方式,D3 CTH使D14能够募集D53,D53进而激活水解酶。通过揭示SCFD 3-D14泛素连接酶中一种意想不到的结构可塑性,我们的研究结果表明E3协调SL信号传导和代谢的复杂机制。
The plant hormone strigolactones (SLs) regulate many aspects of plant physiology. In shoot branching inhibition, the SL-metabolizing α/β hydrolase D14 interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. Despite multiple modes of D14-SL interactions determined recently, how the hydrolase functions with D3 to mediate hormone-dependent D53 ubiquitination remains elusive. Here we show that D3 features a C-terminal α-helix (CTH), which can switch between two conformational states. Distinct from its engaged form, which facilitate the binding of D3 and D14 with a hydrolyzed SL intermediate, the dislodged D3 CTH can recognize unmodified D14 in an open conformation and inhibits its enzymatic activity. In an SL-dependent manner, the D3 CTH enables D14 to recruit D53, which in turn activates the hydrolase. By unraveling an unexpected structural plasticity in SCFD3-D14 ubiquitin ligase, our results suggest an intricate mechanism by which the E3 coordinates SL signaling and metabolism.
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