蛋白质的泛素化修饰在减数分裂过程中发挥了重要的调控作用，作为泛素化体系当中的重要新成员，泛素链延长因子E4(Ufd2)在减数分裂过程中的作用和机制尚待研究。本项目将以酵母为模型研究Ufd2在减数分裂过程中的作用，以离体重建的E4体系为基础，研究E4在底物泛素化过程中的分子机制，从而加深我们对E4本质的认识。同时通过多种途径寻找其在减数分裂过程中的底物及与其互作的蛋白因子，探讨E4对这些蛋白稳定性及功能的影响以期阐明E4在减数分裂过程中的作用机制。

Protein ubiquitylation plays a critical role in meiosis and gametogenesis. However, as a newly defined factor of the ubiquitin-proteasome system, the function of E4 (Ufd2) in meiosis and the underlying mechanism still need to be investigated. We will use budding yeast as a model to study the function of Ufd2 in meiosis, reconstitute the in vitro E4 ubiquitylation system to dissect the mechanism underlying substrate polyubiquitylation, use various biochemical methods to identify the possible substrates/interaction proteins of Ufd2 during meiosis, investigate their relationship with Ufd2 and their effects on meiosis, finally uncover the role of E4 in meiosis and underlying mechanism.