生物
多晶硅
外套
劈理(地质)
精子
透明带
细胞生物学
人类受精
后转座子
蛋白质亚单位
蛋白酵素
生物物理学
遗传学
生物化学
胚胎
卵母细胞
基因组
酶
基因
转座因子
断裂(地质)
古生物学
作者
Shunsuke Nishio,Chihiro Emori,B. Wiseman,Dirk Fahrenkamp,Elisa Dioguardi,Sara Zamora-Caballero,Marcel Bokhove,Ling Han,Alena Stsiapanava,Blanca Algarra,Yonggang Lu,Mayo Kodani,Rachel E. Bainbridge,Kayla M. Komondor,Anne E. Carlson,Michael Landreh,Daniele de Sanctis,Shigeki Yasumasu,Masahito Ikawa,Luca Jovine
出处
期刊:Cell
[Elsevier]
日期:2024-03-01
卷期号:187 (6): 1440-1459.e24
标识
DOI:10.1016/j.cell.2024.02.013
摘要
Following the fertilization of an egg by a single sperm, the egg coat or zona pellucida (ZP) hardens and polyspermy is irreversibly blocked. These events are associated with the cleavage of the N-terminal region (NTR) of glycoprotein ZP2, a major subunit of ZP filaments. ZP2 processing is thought to inactivate sperm binding to the ZP, but its molecular consequences and connection with ZP hardening are unknown. Biochemical and structural studies show that cleavage of ZP2 triggers its oligomerization. Moreover, the structure of a native vertebrate egg coat filament, combined with AlphaFold predictions of human ZP polymers, reveals that two protofilaments consisting of type I (ZP3) and type II (ZP1/ZP2/ZP4) components interlock into a left-handed double helix from which the NTRs of type II subunits protrude. Together, these data suggest that oligomerization of cleaved ZP2 NTRs extensively cross-links ZP filaments, rigidifying the egg coat and making it physically impenetrable to sperm.
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