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Updated: Feb 4, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
A Lotus japonicus E3 ligase interacts with the Nod Factor Receptor 5 and positively regulates nodulation
Daniela Tsikou1,2, Estrella E Ramirez2, Ioanna S Psarrakou1
1Department of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500, Larisa, Greece.
Background:
Post-translational modification of receptor proteins is involved in activation and de-activation of signalling systems in plants. Both ubiquitination and deubiquitination have been implicated in plant interactions with pathogens and symbionts.
Results:
Here we present LjPUB13, a PUB-ARMADILLO repeat E3 ligase that specifically ubiquitinates the kinase domain of the Nod Factor receptor NFR5 and has a direct role in nodule organogenesis events in Lotus japonicus. Phenotypic analyses of three LORE1 retroelement insertion plant lines revealed that pub13 plants display delayed and reduced nodulation capacity and retarded growth. LjPUB13 expression is spatially regulated during symbiosis with Mesorhizobium loti, with increased levels in young developing nodules.
Conclusion:
LjPUB13 is an E3 ligase with a positive regulatory role during the initial stages of nodulation in L. japonicus.
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