中文摘要：

蛋白质的泛素化是一种重要的翻译后修饰过程,参与调控细胞周期、基因转录、信号转导、炎症反应和干细胞的维持等过程。泛素连接酶E3（ubiqutin ligase）是泛素化过程中关键酶。但许多E3基因在发育中的功能和作用机制还不明确。该研究以黑腹果蝇为模式动物,研究泛素连接酶家族一个重要基因CG4911的功能及分子机制。获得CG4911基因敲除果蝇,CG4911敲除果蝇纯合子可活。原位杂交结果显示,CG4911在胚胎发育早期表达。通过构建CG4911-pUAST-3HA重组子转染Hela细胞,确定CG4911定位于细胞质中,其表达并无修饰作用,并且过表达基因CG4911可导致背板发育缺陷。该研究首次获得了CG4911基因敲除果蝇和CG4911转基因果蝇,并初步探索了F-box基因CG4911的功能,为进一步阐明泛素连接酶的功能及分子机制提供了科学依据。

英文摘要：

Protein ubiquitination is an important post-translational modification process involved in cell cycle regulation,gene transcription,signal transduction,inflammation and stem cell maintenance.Ubiqutin ligase E3 is an essential enzyme and plays important role in ubiquitin-proteasome process.However,little is known about its function and molecular mechanism of E3 ligase during development.In this study,Drosophila melanogaster was used as a model to study the function and molecular mechanism of gene CG4911,which is one of the important ubiquitin ligases genes.We have generated mutant for CG4911 and construct CG4911-pUAST-V5 vector as well as its transgenic lines.The result showed that CG4911 mutant is viable.The protein of CG4911 localized in the cytoplasm and there was no modification happened with CG4911 when expressed in Hela cells.Furthermore,over expression of CG4911 leads to the notum developmental defects.In summary,this is the first time to get CG4911 knock out mutant and CG4911 transgenic fly.Also,it’s the first time to uncover a novel F-box gene CG4911 gene function in developmental contaxts.Our studies provide basis to further clarify the function of ubiquitin ligases and molecular mechanisms.