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Updated: Jun 13, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
Structural and functional studies of SIZ1, a PIAS-type SUMO E3 ligase from Arabidopsis
Mi Sun Cheong1, Hyeong Cheol Park1, Hans J Bohnert1
1Division of Applied Life Science (BK21 program), PMBBRC, EB-NCRC, Gyeongsang National University, Jinju, Korea.
Abstract:
Small ubiquitin-like modifier (SUMO) is a post-translational modifier peptide that is involved in several biological processes in eukaryotes. Arabidopsis SIZ1, a SUMO E3 ligase, is an ortholog of the mammalian PIAS (Protein Inhibitor of Activated STAT) and yeast SIZ (SAP/Miz) proteins. SIZ1 contains all of the typical domains of PIAS/SIZ-type proteins, such as the PINIT, SAP, SP-RING, and plant-specific PHD domains. SIZ1 plays a pivotal role in controlling SUMOylation, and disruption of its function has been reported to affect stress responses, growth, and development. We performed a structural and functional analysis of SIZ1 by determining the phenotypes of siz1 knockout mutants transformed with SIZ1 alleles carrying point mutations in predicted SIZ1 domains. This study establishes that the diverse properties characteristic of SIZ1 are associated with specific domains and that they can be separated.
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