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PNAS:拟南芥DELLA蛋白的非经典降解途径

已有 459 次阅读 2020-6-1 11:06 |个人分类:每日摘要|系统分类:论文交流

COP1 destabilizes DELLA proteins in Arabidopsis

第一作者Noel Blanco-Touriñán

第一单位西班牙瓦伦西亚理工大学

通讯作者David Alabadί


 Abstract 


背景回顾DELLA transcriptional regulators are central components in the control of plant growth responses to the environment. This control is considered to be mediated by changes in the metabolism of the hormones gibberellins (GAs), which promote the degradation of DELLAs.


提出问题:However, here we show that warm temperature or shade reduced the stability of a GA-insensitive DELLA allele in Arabidopsis thaliana.


初步发现:Furthermore, the degradation of DELLA induced by the warmth preceded changes in GA levels and depended on the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1).


试验结果:COP1 enhanced the degradation of normal and GA-insensitive DELLA alleles when coexpressed in Nicotiana benthamiana. DELLA proteins physically interacted with COP1 in yeast, mammalian, and plant cells. This interaction was enhanced by the COP1 complex partner SUPRESSOR OF phyA-105 1 (SPA1). The level of ubiquitination of DELLA was enhanced by COP1 and COP1 ubiquitinated DELLA proteins in vitro.


结论:We propose that DELLAs are destabilized not only by the canonical GA-dependent pathway but also by COP1 and that this control is relevant for growth responses to shade and warm temperature.


 摘  要 


DELLA转录调控子是控制响应环境时植物生长的核心组分。DELLA控制的植物生长通常是由植物激素赤霉素GA代谢变化所介导的,GA能够促进DELLA蛋白的降解。然而,作者发现温暖的温度下或者是遮阴都会减少拟南芥中GA不敏感的DELLA等位蛋白的稳定性。此外,由温暖诱导的DELLA降解要快于GA水平的变化,并且依赖于E3泛素连接酶COP1。在烟草中共表达时,COP1能够增强正常和GA不敏感型DELLA等位蛋白的降解。在酵母、哺乳动物和植物细胞中,DELLA蛋白均能够与COP1发生物理互作。并且这种互作能够被COP1复合伴侣SPA1增强。另外,COP1能够增强DELLA蛋白的泛素化水平,并且体外试验中COP1能够泛素化DELLA蛋白。因此,本文的研究显示DELLA蛋白不仅会被经典的GA依赖性途径所降解,还会被COP1泛素化、降解,并且这种控制与植物对阴影和温暖环境的生长响应有关。



doi: 10.1073/pnas.1907969117


Journal: PNAS

First Published: May 29, 2020



http://blog.sciencenet.cn/blog-3158122-1235900.html

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