GID2, an F-box subunit of the SCF E3 complex, specifically interacts with phosphorylated SLR1 protein and regulates the gibberellin-dependent degradation of SLR1 in rice
GID2, an F-box subunit of the SCF E3 complex, specifically interacts with phosphorylated SLR1 protein and regulates the gibberellin-dependent degradation of SLR1 in rice
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DOI：
10.1111/j.1365-313x.2003.01990.x
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发表时间：
2004-02-01
期刊：
影响因子：
7.2
通讯作者：
Matsuoka, M
中科院分区：
文献类型：
--
作者：
Gomi, K;Sasaki, A;Matsuoka, M
植物激素赤霉素（GA）控制着植物的生长和发育。此前，我们鉴定出一种水稻F - 盒蛋白，即赤霉素不敏感矮化2（GID2），它对赤霉素介导的DELLA蛋白降解至关重要。在本研究中，我们分析了GID2的生物学和分子生物学特性。GID2优先在积极合成赤霉素的水稻器官中表达。对GID2的结构域分析表明，其C末端区域对GID2的功能至关重要，而N末端区域则不然。酵母双杂交试验和免疫沉淀实验证明，GID2通过与水稻ASK1同源物OsSkp15相互作用，是SCF复合物的一个组分。此外，体外下拉试验显示，GID2与磷酸化的细秆稻1（SLR1）特异性相互作用。综合这些结果，我们得出结论：磷酸化的SLR1通过GID2与磷酸化的SLR1之间的相互作用亲和力被SCFGID2复合物捕获，从而引发SLR1的泛素介导的降解。
The phytohormone gibberellin (GA) controls growth and development in plants. Previously, we identified a rice F-box protein, gibberellin-insensitive dwarf2 (GID2), which is essential for GA-mediated DELLA protein degradation. In this study, we analyzed the biological and molecular biological properties of GID2. Expression of GID2 preferentially occurred in rice organs actively synthesizing GA. Domain analysis of GID2 revealed that the C-terminal regions were essential for the GID2 function, but not the N-terminal region. Yeast two-hybrid assay and immunoprecipitation experiments demonstrated that GID2 is a component of the SCF complex through an interaction with a rice ASK1 homolog, OsSkp15. Furthermore, an in vitro pull-down assay revealed that GID2 specifically interacted with the phosphorylated Slender Rice 1 (SLR1). Taken these results together, we conclude that the phosphorylated SLR1 is caught by the SCFGID2 complex through an interacting affinity between GID2 and phosphorylated SLR1, triggering the ubiquitin-mediated degradation of SLR1.