Moa1与CENP-C和Rec8的相互作用及其在裂殖酵母减数分裂中的功能

Functional roles of the interaction of Moa1 with

减数分裂特异性调控分子Moa1定位到着丝粒受到动粒蛋白CENP-C的调控,同时Moa1参与黏连蛋白Rec8介导的着丝粒区域姐妹染色单体的黏连。为了研究这些蛋白质之间的相互作用,本研究利用酵母双杂交实验(yeast two-hybrid assay)测定分析了Moa1和CENP-C、Rec8之间的相互作用,并通过在Moa1中定点突变鉴定了与CENP-C和Rec8相互作用所需的一些氨基酸残基。实验结果表明,Moa1和CENP-C的相互作用对于Moa1参与调节姐妹动粒的单极附着很重要。然而,双杂交实验中与Rec8相互作用所需的Moa1的S143和T150突变没有显示出Moa1或Rec8功能的显著缺陷。这表明氨基酸残基的突变可能不足以干扰体内Moa1和Rec8之间的相互作用,需要进一步的研究来确定Moa1和Rec8的相互作用域。本研究揭示了影响减数分裂同源染色体分离的Moa1氨基酸位点,为减数分裂的染色体分离机制提供更深入的理解。

The localization of the meiotic specific regulatory molecule Moa1 to the centromere is regulated by the kinetochore protein CENP-C,and participates in the cohesion of sister chromatids in the centromere region mediated by the cohesin Rec8.To examine the interaction of these proteins,we analyzed the interactions between Moa1 and Rec8,CENP-C by yeast two-hybrid assays and identified several amino acid residues in Moa1 required for the interaction with CENP-C and Rec8.The results revealed that the interaction between Moa1 and CENP-C is crucial for the Moa1 to participate in the regulation of monopolar attachment of sister kinetochores.However,mutation at S143 and T150 of Moa1,which are required for interaction with Rec8 in the two-hybrid assay,did not show significant defects.Mutations in amino acid residues may not be sufficient to interfere with the interaction between Moa1 and Rec8 in vivo.Further research is needed to determine the interaction domain between Moa1 and Rec8.This study revealed specific amino acid sites at which Moa1 affects the meiotic homologous chromosome segregation,providing a deeper understanding of the mechanism of meiotic chromosome segregation.