Identification of distinctive interdomain interactions among ZP-N, ZP-C and other domains of zona pellucida glycoproteins underlying association of chicken egg-coat matrix.
Identification of distinctive interdomain interactions among ZP-N, ZP-C and other domains of zona pellucida glycoproteins underlying association of chicken egg-coat matrix.
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DOI：
10.1016/j.fob.2015.05.005
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发表时间：
2015
期刊：
影响因子：
2.6
通讯作者：
Ujita, Minoru
中科院分区：
文献类型：
--
作者：
Okumura, Hiroki;Sato, Takahiro;Sakuma, Rio;Fukushima, Hideaki;Matsuda, Tsukasa;Ujita, Minoru
鸡ZP 1和ZP 3通过它们的ZP-C结构域之间的强相互作用组装。鸡ZP 1和ZP 3的ZP-C结构域深深嵌入在蛋壳基质中。鸡ZP 1通过重复结构域之间的非共价相互作用形成同源复合物。鸡ZPD沉积在ZP 1-ZP 3基质的空隙中。我们提出了一个模型，从这些结果的鸡蛋壳矩阵的架构。脊椎动物卵被，包括哺乳动物卵透明膜，是卵母细胞特异性的细胞外基质，包含2至6个卵透明膜（ZP）糖蛋白。卵被在受精过程中起着重要作用，尤其是在与精子的物种特异性相互作用中，诱导精子顶体反应，形成多精受精的障碍。有人建议，介导和/或协调调节的生理功能的卵外壳的肽和碳水化合物部分的ZP糖蛋白，在空间上排列在卵外壳，而脊椎动物卵外壳基质的架构的全面理解仍然难以捉摸。在这里，我们推导出的方向和/或分布的鸡ZP糖蛋白，ZP 1，ZP 3和ZPD，在蛋壳基质共聚焦免疫荧光显微镜，并在ZP 1-ZP 3复合物在体外产生的免疫共沉淀测定。我们进一步证实了ZP糖蛋白的结构域间的相互作用，通过远Western印迹分析的鸡蛋外壳蛋白和ZP 1在血清中的下拉测定，使用ZP糖蛋白的重组结构域作为探针。我们的研究结果表明，ZP 1和ZP 3通过其ZP-C结构域结合，形成ZP 1-ZP 3复合物和原纤维，它们通过ZP 1的重复结构域之间的相互作用组装成束，形成ZP 1-ZP 3基质，并且ZPD分子通过其ZP-N和ZP-C结构域自缔合并结合到ZP 1-ZP 3基质，形成蛋壳基质。基于这些结果，我们提出了一个可能适用于其他脊椎动物的鸡蛋外套矩阵的架构的尝试性模型。
Chicken ZP1 and ZP3 assemble through strong interactions between their ZP-C domains. ZP-C domains of chicken ZP1 and ZP3 are deeply embedded in the egg-coat matrix. Chicken ZP1 forms a homocomplex through non-covalent interaction between repeat domains. Chicken ZPD is deposited on the interstices of ZP1–ZP3 matrix in the egg coat. We propose a model for the architecture of chicken egg-coat matrix from these results. The vertebrate egg coat, including mammalian zona pellucida, is an oocyte-specific extracellular matrix comprising two to six zona pellucida (ZP) glycoproteins. The egg coat plays important roles in fertilization, especially in species-specific interactions with sperm to induce the sperm acrosome reaction and to form the block to polyspermy. It is suggested that the physiological functions of the egg coat are mediated and/or regulated coordinately by peptide and carbohydrate moieties of the ZP glycoproteins that are spatially arranged in the egg coat, whereas a comprehensive understanding of the architecture of vertebrate egg-coat matrix remains elusive. Here, we deduced the orientations and/or distributions of chicken ZP glycoproteins, ZP1, ZP3 and ZPD, in the egg-coat matrix by confocal immunofluorescent microscopy, and in the ZP1–ZP3 complexes generated in vitro by co-immunoprecipitation assays. We further confirmed interdomain interactions of the ZP glycoproteins by far-Western blot analyses of the egg-coat proteins and pull-down assays of ZP1 in the serum, using recombinant domains of ZP glycoproteins as probes. Our results suggest that the ZP1 and ZP3 bind through their ZP-C domains to form the ZP1–ZP3 complexes and fibrils, which are assembled into bundles through interactions between the repeat domains of ZP1 to form the ZP1–ZP3 matrix, and that the ZPD molecules self-associate and bind to the ZP1–ZP3 matrix through its ZP-N and ZP-C domains to form the egg-coat matrix. Based on these results, we propose a tentative model for the architecture of the chicken egg-coat matrix that might be applicable to other vertebrate ones.
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影响因子：
5.8
作者：
Callebaut, Isabelle;Mornon, Jean-Paul;Monget, Philippe
通讯作者：
Monget, Philippe
影响因子：
3.5
作者：
BORK, P;SANDER, C
通讯作者：
SANDER, C
影响因子：
64.5
作者：
Ensslin, MA;Shur, BD
通讯作者：
Shur, BD
影响因子：
4.8
作者：
Bausek, N;Waclawek, M;Wohlrab, F
通讯作者：
Wohlrab, F
DOI：
10.1073/pnas.0401600101
发表时间：
2004-04-20
影响因子：
11.1
作者：
Jovine, L;Qi, HY;Wassarman, PM
通讯作者：
Wassarman, PM