Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes
Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes
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DOI：
10.1101/gad.1229504
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发表时间：
2004-09-01
影响因子：
10.5
通讯作者：
Deng, XW
中科院分区：
文献类型：
--
作者：
Yanagawa, Y;Sullivan, JA;Deng, XW
COP10是一种泛素偶联酶变体（UEV），被认为在拟南芥中与COP1、DET1和COP9信号体（CSN）一起抑制光形态发生。在这里，我们证明了COP10在体内与泛素偶联酶（E2s）相互作用，并可以增强其在体外的活性，这种活性不同于先前表征的UEVs，如MMS2和UEV1。此外，我们发现COP10与紫外线损伤的dna结合蛋白la （DDB1a）和去黄化蛋白1 （DET1）形成复合物，并与COPI发生物理相互作用。和CSN。纯化的CDD （COP10, DDB1, DET1）复合物也显示出E2活性（UEA）的增强，与COP10本身相似。我们的数据表明，COP10与COPI和CSN一起，通过泛素/26S蛋白酶体系统促进光形态发生的正调节因子（如转录因子HY5）的降解。因此，CDD复合物可能作为一种泛素化促进因子来调节光形态发生。
COP10 is a ubiquitin-conjugating enzyme variant (UEV), which is thought to act together with COP1, DET1, and the COP9 signalosome (CSN) in Arabidopsis to repress photomorphogenesis. Here, we demonstrate that COP10 interacts with ubiquitin-conjugating enzymes (E2s) in vivo, and can enhance their activity in vitro, an activity distinct from previous characterized UEVs such as MMS2 and UEV1. Furthermore, we show that COP10 forms a complex with UV-damaged DNA-binding protein la (DDB1a) and de-etiolated 1 (DET1), and physically interacts with COPI. and the CSN. Purified CDD (COP10, DDB1, DET1) complex also shows enhancement of E2 activity (UEA) similar to that observed with COP10 itself. Our data suggests that COP10, along with COPI and the CSN, promotes the degradation of positive regulators of photomorphogenesis, such as the transcription factor HY5, via the ubiquitin/26S proteasome system. Thus, the CDD complex may act as a ubiquitylation-promoting factor to regulate photomorphogenesis.