Structural plasticity of D3–D14 ubiquitin ligase in strigolactone signalling

Nitzan Shabek, Fabrizio Ticchiarelli, Haibin Mao, Thomas R. Hinds, Ottoline Leyser and Ning Zheng ()
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Nitzan Shabek: University of Washington
Fabrizio Ticchiarelli: University of Cambridge
Haibin Mao: University of Washington
Thomas R. Hinds: University of Washington
Ottoline Leyser: University of Cambridge
Ning Zheng: University of Washington

Nature, 2018, vol. 563, issue 7733, 652-656

Abstract: Abstract The strigolactones, a class of plant hormones, regulate many aspects of plant physiology. In the inhibition of shoot branching, the α/β hydrolase D14—which metabolizes strigolactone—interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. Despite the fact that multiple modes of interaction between D14 and strigolactone have recently been determined, how the hydrolase functions with D3 to mediate hormone-dependent D53 ubiquitination remains unknown. Here we show that D3 has a C-terminal α-helix that can switch between two conformational states. The engaged form of this α-helix facilitates the binding of D3 and D14 with a hydrolysed strigolactone intermediate, whereas the dislodged form can recognize unmodified D14 in an open conformation and inhibits its enzymatic activity. The D3 C-terminal α-helix enables D14 to recruit D53 in a strigolactone-dependent manner, which in turn activates the hydrolase. By revealing the structural plasticity of the SCFD3–D14 ubiquitin ligase, our results suggest a mechanism by which the E3 coordinates strigolactone signalling and metabolism.

Keywords: Strigolactone Signaling; Shoot Branching; Open Conformation; Xl Sm; Hanging Drop Vapor Diffusion Method (search for similar items in EconPapers)
Date: 2018
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DOI: 10.1038/s41586-018-0743-5

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