2014年第41卷第7期目录
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封面故事:在早期胚胎发育过程中,卵母细胞中的许多母性效应因子发挥着至关重要的作用.Filia蛋白作为众多母性效应因子中的一种,是皮质下母性效应因子复合体(SCMC)的组成蛋白.母源Filia蛋白对于保持染色体以整倍体形式存在起关键作用.此外,母源Filia 蛋白能够确保早期胚胎发育进程的正常进行.Filia蛋白N端含有一个非典型的KH结构域,该结构域能够结合RNA,可能在转录调控过程中发挥作用.卵母细胞中含有谷胱甘肽(GSH),GSH含量的变化是卵母细胞成熟程度的指标.刘新奇研究组在含有GSH环境中得到了Filia N端1~124个氨基酸蛋白的一种新型晶体结构,与在不含GSH环境中生长的晶体相比,该结构中蛋白间相互作用方式及晶体堆积方式存在较大差异,这种二聚体向十聚体的结构转变为进一步研究不同生理条件下Filia蛋白的结构与功能奠定了结构基础.
(李新新,王巨克,刘新奇. 鼠源Filia N端蛋白在GSH条件中的一种全新三维结构,本期第666~673页)
Cover Story:Filia is one of the components of maternal Subcortical Maternal Complex(SCMC). The N-terminal of Filia is similar to KH domain of type I family, which play roles in transcription regulation in oogenesis and embryo development by binding RNA. Additionally, maternal Filia plays essential role in maintaining euploidy. The absence of maternal Filia appears to delay embryonic progression, which can decrease the number of offspring rather than sterile. During oocyte maturation stage, the concentration of GSH varied to keep balance of oxidation-reduction. Our crystallographic studies successfully reveal the structure of Filia N-terminal protein grown in solution with GSH. In contrast with the structure of Filia N-terminal protein grown in condition free of GSH, protein grown in GSH have five pairs of dimer in an asymmetry unit. Domain swapping occurs in the α3-helix of Filia (N1-124) molecules. A special decamer structure is formed by ionic interaction, H-bond and hydrophobic interaction. The Filia N-terminal structure provides a structural foundation for further researches on the structure and function of Filia in diversity physiological environment.
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综述与专论
研究报告
技术与方法
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