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Updated: Oct 10, 2025

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
Functional characterization of three maize SIZ/PIAS-type SUMO E3 ligases
Ruiqiang Lai1, Jieming Jiang1, Jun Wang1
1Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou, 510631, China.
Abstract:
SUMOylation is a critical post-translational modification that regulates the nature and activity of protein substrates. The reaction is usually enhanced by a SIZ/PIAS-type of SUMO E3 ligase, but the functions of its homologs in maize have not yet been reported. In this study, we functionally characterized three members of this family of SUMO ligases, ZmSIZ1a, ZmSIZ1b, and ZmSIZ1c, from Zea mays. These maize SIZ1 homologs harbor conserved domains and structures with AtSIZ1, suggesting that they are potential functional SUMO ligases, which is supported by further biochemical data. The expression of these maize SIZ1 genes was detectable ubiquitously in different maize tissues and was usually induced by abiotic stresses. Expression of ZmSIZ1 members complements the leaf developmental defects of the AtSIZ1 mutant, suggesting their conserved function in development regulation. Interestingly, overexpression of ZmSIZ1c, but not ZmSIZ1a or ZmSIZ1b, in the wild-type Arabidopsis resulted in early flowering, implying that these members differ in terms of flowering control. Besides, overexpression of these ZmSIZ1 genes also improved salt tolerance in Arabidopsis. Collectively, our functional characterization of the ZmSIZ1 members provides hints for further investigation on the functions of SUMOylation in the development and stress responses in maize.
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