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鉴定应激反应中 RAP2.4 相关蛋白的特性及其作为 CUL3 依赖性 E3 连接酶底物的作用。

Characterization of RAP2.4-Related Proteins in Stress Response and as CUL3-Dependent E3 Ligase Substrates.

机构信息

School of Biological Sciences, Washington State University, Pullman, WA 99164, USA.

出版信息

Cells. 2019 Apr 10;8(4):336. doi: 10.3390/cells8040336.

Abstract

The turnip has important economic value and represents a good model system to study gene function in crop plants. ERF/AP2 transcription factors are a major group of proteins that are often involved in regulating stress-responses and developmental programs. Some ERF/AP2 proteins are targets of CULLIN3-based E3 ligases that use BTB/POZ-MATH proteins as substrate receptors. These receptors bind the transcription factor and facilitate their ubiquitylation and subsequent degradation via the 26S proteasome. Here, we show tissue and stress-dependent expression patterns for three ERF/AP2 proteins that are closely related to AtRAP2.4. Cloning of the genes showed that the corresponding proteins can assemble with a BPM protein and CULLIN3, and that they are instable in a 26S proteasome dependent manner. This work demonstrates the conserved nature of the ERF/AP2-CULLIN3-based E3 ligase interplay, and represents a first step to analyze their function in a commercially relevant crop plant.

摘要

芜菁具有重要的经济价值,是研究作物中基因功能的良好模式系统。ERF/AP2 转录因子是一类重要的蛋白质,通常参与调节应激反应和发育程序。一些 ERF/AP2 蛋白是基于 CULLIN3 的 E3 连接酶的靶标,该酶使用 BTB/POZ-MATH 蛋白作为底物受体。这些受体结合转录因子,促进它们通过 26S 蛋白酶体的泛素化和随后的降解。在这里,我们展示了三个与 AtRAP2.4 密切相关的 ERF/AP2 蛋白的组织和应激依赖性表达模式。基因克隆表明,相应的蛋白可以与 BPM 蛋白和 CULLIN3 组装,并且它们以依赖 26S 蛋白酶体的方式不稳定。这项工作证明了 ERF/AP2-基于 CULLIN3 的 E3 连接酶相互作用的保守性质,并且代表了在商业上相关的作物植物中分析其功能的第一步。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/918d/6523098/32fd5eccfc72/cells-08-00336-g001.jpg

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