Cheong Mi Sun, Park Hyeong Cheol, Bohnert Hans J, Bressan Ray A, Yun Dae-Jin
Division of Applied Life Science (BK21 program), PMBBRC, EB-NCRC, Gyeongsang National University, Jinju, Korea.
Plant Signal Behav. 2010 May;5(5):567-9. doi: 10.4161/psb.11426. Epub 2010 Apr 20.
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.
小泛素样修饰物（SUMO）是一种参与真核生物多种生物学过程的翻译后修饰肽。拟南芥SIZ1是一种SUMO E3连接酶，是哺乳动物PIAS（活化STAT的蛋白抑制剂）和酵母SIZ（SAP/Miz）蛋白的直系同源物。SIZ1包含PIAS/SIZ型蛋白的所有典型结构域，如PINIT、SAP、SP-RING和植物特异性PHD结构域。SIZ1在控制SUMO化过程中起关键作用，据报道其功能破坏会影响应激反应、生长和发育。我们通过确定用在预测的SIZ1结构域中携带点突变的SIZ1等位基因转化的siz1敲除突变体的表型，对SIZ1进行了结构和功能分析。这项研究表明，SIZ1的多种特性与特定结构域相关，并且它们可以被分离。
