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Pré-Publication, Document De Travail Année : 2022

Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators

Zhishuo Wang
  • Fonction : Auteur
Beatriz Orosa-Puente
Mika Nomoto
Heather Grey
  • Fonction : Auteur
Takakazu Matsuura
  • Fonction : Auteur
Izumi Mori
Yasuomi Tada
Steven Spoel

Résumé

Abstract The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains unknown. We report that in Arabidopsis the salicylic acid-and ethylene-responsive TAs, NPR1 and EIN3, are relayed from pathway-specific ubiquitin ligases to proteasome-associated HECT-type UPL3/4 ligases. Activity and stability of NPR1 was regulated by sequential action of three ubiquitin ligases, including UPL3/4, while proteasome processing of EIN3 required physical handover between ethylene-responsive SCF EBF2 and UPL3/4 ligases. Consequently, UPL3/4 controlled extensive hormone-induced developmental and stress-responsive transcriptional programmes. Thus, our findings identify unknown ubiquitin ligase relays that terminate with proteasome-associated HECT-type ligases, which may be a universal mechanism for processive degradation of proteasome-targeted TAs and other substrates. One-Sentence Summary Transcriptional activators are targeted by proteasomal ubiquitin ligase relays that control their activity and stability.
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Dates et versions

hal-03441849 , version 1 (08-11-2022)

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Zhishuo Wang, Beatriz Orosa-Puente, Mika Nomoto, Heather Grey, Thomas Potuschak, et al.. Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators. 2022. ⟨hal-03441849⟩
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