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The F-box domain is a conserved structural protein motif that most frequently interacts with the SKP1 protein, the core of the SCFs (SKP1-CULLIN-F-box protein ligase) E3 ubiquitin protein ligases. As part of the SCF complexes, the various F-box proteins recruit substrates for degradation through ubiquitination. In this study, we functionally characterized an F-box gene (MtF-box) identified earlier in a population of Tnt1 retrotransposon-tagged mutants of Medicago truncatula and its Arabidopsis thaliana homolog (AtF-box) using gain- and loss-of-function plants. We highlighted the importance of MtF-box in leaf development of M. truncatula. Protein-protein interaction analyses revealed the 2-isopropylmalate synthase (IPMS) protein as a common interactor partner of MtF-box and AtF-box, being a key enzyme in the biosynthesis pathway of the branched-chain amino acid leucine. For further detailed analysis, we focused on AtF-box and its role during the cell division cycle. Based on this work, we suggest a mechanism for the role of the studied F-box gene in regulation of leucine homeostasis, which is important for growth. © 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.


Anelia Iantcheva, Miroslava Zhiponova, Miglena Revalska, Jefri Heyman, Ivayla Dincheva, Ilian Badjakov, Nathan De Geyter, Irina Boycheva, Sofie Goormachtig, Lieven De Veylder. A common F-box gene regulates the leucine homeostasis of Medicago truncatula and Arabidopsis thaliana. Protoplasma. 2022 Mar;259(2):277-290

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PMID: 33973099

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