Thioredoxin-dependent disulfide bond reduction is required for protamine eviction from sperm chromatin.
Thioredoxin-dependent disulfide bond reduction is required for protamine eviction from sperm chromatin.
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DOI：
10.1101/gad.290916.116
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发表时间：
2016-12-15
影响因子：
10.5
通讯作者：
Fyodorov DV
中科院分区：
文献类型：
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作者：
Emelyanov AV;Fyodorov DV
Emelyanov和Fyodorov发现果蝇硫氧还蛋白死头(DHD)是导致精蛋白分子间二硫键减少并在受精过程中将其逐出精子的因素。鱼精蛋白中的半胱氨酸氧化导致它们的寡聚，并有助于精子染色质的紧致。在这里，我们确定果蝇硫氧还蛋白死头(DHD)是导致精蛋白分子间二硫键减少并在受精过程中将其逐出精子的因素。只有当鱼精蛋白低聚物第一次被DHD转化为单体时，鱼精蛋白伴侣TAP/p32才能在体外解离DNA-鱼精蛋白复合体。DHD缺失的胚胎在第一次原核分裂后不能解聚精子染色质并终止发育。因此，硫氧还蛋白DHD在早期发育中起着关键作用，促进精子染色质结构从鱼精蛋白向体细胞核小体染色质的转换。
Emelyanov and Fyodorov identify the Drosophila thioredoxin Deadhead (DHD) as the factor responsible for the reduction of intermolecular disulfide bonds in protamines and their eviction from sperm during fertilization. Cysteine oxidation in protamines leads to their oligomerization and contributes to sperm chromatin compaction. Here we identify the Drosophila thioredoxin Deadhead (DHD) as the factor responsible for the reduction of intermolecular disulfide bonds in protamines and their eviction from sperm during fertilization. Protamine chaperone TAP/p32 dissociates DNA–protamine complexes in vitro only when protamine oligomers are first converted to monomers by DHD. dhd-null embryos cannot decondense sperm chromatin and terminate development after the first pronuclear division. Therefore, the thioredoxin DHD plays a critical role in early development to facilitate the switch from protamine-based sperm chromatin structures to the somatic nucleosomal chromatin.