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首页> 外文期刊>Cell and Tissue Research >Identification and characterization of RING-finger ubiquitin ligase UBR7 in mammalian spermatozoa
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Identification and characterization of RING-finger ubiquitin ligase UBR7 in mammalian spermatozoa

机译：哺乳动物精子中环手指泛素立角酶UBr7的鉴定与表征

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The ubiquitin-proteasome system (UPS) controls intracellular protein turnover in a substrate-specific manner via E3-type ubiquitin ligases. Mammalian fertilization and particularly sperm penetration through the oocyte vitelline coat, the zona pellucida (ZP), is regulated by UPS. We use an extrinsic substrate of the proteasome-dependent ubiquitin-fusion degradation pathway, the mutant ubiquitin UBB+1, to provide evidence that an E3-type ligase activity exists in sperm-acrosomal fractions. Protein electrophoresis gels from such de novo ubiquitination experiments contained a unique protein band identified by tandem mass spectrometry as being similar to ubiquitin ligase UBR7 (alternative name: C14ORF130). Corresponding mRNA was amplified from boar testis and several variants of the UBR7 protein were detected in boar, mouse and human sperm extracts by Western blotting. Genomic analysis indicated a high degree of evolutionary conservation, remarkably constant purifying selection and conserved testis expression of the UBR7 gene. By immunofluorescence, UBR7 was localized to the spermatid acrosomal cap and sperm acrosome, in addition to hotspots of proteasomal activity in spermatids, such as the cytoplasmic lobe, caudal manchette, nucleus and centrosome. During fertilization, UBR7 remained with the ZP-bound acrosomal shroud following acrosomal exocytosis. Thus, UBR7 is present in the acrosomal cap of round spermatids and within the acrosomal matrix of mature boar spermatozoa. These data provide the first evidence of ubiquitin ligase activity in mammalian spermatozoa and indicate UBR7 involvement in spermiogenesis.
机译：泛素 - 蛋白酶体系（UPS）通过E3型泛素连接酶控制以底物特异性方式控制细胞内蛋白质转换。哺乳动物施肥，特别是精子渗透通过卵母细胞vitelline涂层，Zona Pellucida（ZP），由UPS调节。我们使用蛋白酶体依赖性泛素融合降解途径，突变体泛素UBB + 1的外素底物，以提供表现出E3型连接酶活性在精子 - 拟素馏分中存在。来自诸如Novo泛素化实验的蛋白质电泳凝胶含有由串联质谱法鉴定的独特的蛋白质带，与泛素连接酶UBr7类似（替代名称：C14ORF130）。通过蛋白质印迹在野猪，小鼠和人体精子提取物中检测到相应的mRNA和UBR7蛋白的几种变体。基因组分析表明了ubr7基因的显着恒定净化选择和保守的睾丸表达。通过免疫荧光，除了精菌中的蛋白酶体活性的热点之外，ubr7局部局限于精菌质帽和精子伪体，例如细胞质叶，尾部植物，核和中心组。在施肥期间，ubr7伴随着ZP结合的辅助剂护罩，伴有仿毒剂外尿作用。因此，UBR7存在于圆形精子的拟囊体盖中，并在成熟的野猪精子的橡皮质基质中存在。这些数据提供了哺乳动物精子中泛素连接酶活性的第一种证据，并表明UBR7参与精子发生。

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