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Related Experiment Video

Updated: Feb 5, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
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Multi-tiered pairing selectivity between E2 ubiquitin-conjugating enzymes and E3 ligases.

Ilona Turek1, Nadine Tischer1, Roman Lassig1

  • 1From the Leibniz Institute of Plant Biochemistry, Independent Junior Research Group, Weinberg 3, 06120 Halle (Saale) and.

The Journal of Biological Chemistry
|September 7, 2018
PubMed
Summary

Ubiquitin conjugation enzymes (E2s) and E3 ligases form specific pairs in plants. This study reveals a multi-tiered system for E2-E3 interactions, crucial for regulating plant immunity.

Keywords:
E3 ubiquitin ligasecell signalinginnate immunityubiquitinubiquitin-conjugating enzyme (E2 enzyme)

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Area of Science:

  • * Molecular Biology
  • * Plant Biology
  • * Biochemistry

Background:

  • * Ubiquitination is a vital post-translational modification regulating cellular processes.
  • * E2 ubiquitin-conjugating enzymes (UBCs) are central to ubiquitination, mediating ubiquitin chain assembly and determining substrate fate.
  • * Specificity in ubiquitination is primarily dictated by E3 ubiquitin ligases, but the precise in vivo interactions between E2 and E3 enzymes are not well understood.

Purpose of the Study:

  • * To investigate the interaction selectivity between 37 Arabidopsis E2s and the U-box E3 ligase PUB22.
  • * To explore the role of different E3 domains in mediating E2-E3 pairing.
  • * To determine how in vivo E2-E3 pairing is modulated during plant immune responses.

Main Methods:

  • * Yeast two-hybrid assays to test interactions between 37 Arabidopsis E2s and PUB22.
  • * Analysis of PUB22 domains (U-box and ARM repeats) for E2 docking specificity.
  • * In vitro autoubiquitination assays to assess E2-E3 activity.
  • * Analysis of E2-E3 pairing dynamics during immune signaling in Arabidopsis.

Main Results:

  • * The U-box domain of PUB22 interacted with 18 out of 37 E2s, while the ARM repeats imposed further specificity, interacting with 11 E2s.
  • * In vitro activity partially reflected in vivo selectivity.
  • * In vivo E2-E3 pairing was dynamic, with UBC30 pairing inhibited and UBC35 pairing increased during immune response.
  • * ubc35 ubc36 mutants exhibited enhanced immune responses, mimicking pub22 pub23 pub24 phenotypes.

Conclusions:

  • * E2-E3 interaction selectivity is governed by a multi-tiered system involving specific E3 domains.
  • * In vivo E2-E3 pairing is dynamic and responsive to cellular signaling, such as immune responses.
  • * The E2-E3 network plays a critical role in regulating plant immunity, highlighting UBC35 and UBC36 in this process.