Protamine-induced condensation and decondensation of the same DNA molecule
Protamine-induced condensation and decondensation of the same DNA molecule
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DOI：
10.1126/science.286.5437.120
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发表时间：
1999-10-01
期刊：
影响因子：
56.9
通讯作者：
Balhorn, R
中科院分区：
文献类型：
--
作者：
Brewer, LR;Corzett, M;Balhorn, R
精子和某些病毒的DNA被富含精氨酸的蛋白质凝聚成环状亚基，这是一种使其整个基因组失活的包装形式。用光学陷阱操纵单个DNA分子，以检查鱼精蛋白及其DNA结合结构域子集Arg结合诱导的环面形成动力学(6)。对lambda-噬菌体DNA的缩聚和去缩聚实验表明，鱼精蛋白中富含精氨酸的锚定结构域的数量影响环状体的形成和稳定性。研究结果解释了为什么精蛋白含有如此多的精氨酸，并表明这些蛋白质必须在受精后主动从精子染色质中去除。
The DNA sperm and certain viruses is condensed by arginine-rich proteins into toroidal subunits, a form of packaging that inactivates their entire genome. Individual DNA molecules were manipulated with an optical trap to examine the kinetics of torus formation induced by the binding of protamine and a subset of its DNA binding domain, Arg(6). Condensation and decondensation experiments with lambda-phage DNA show that toroid formation and stability are influenced by the number of arginine-rich anchoring domains in protamine. The results explain why protamines contain so much arginine and suggest that these proteins must be actively removed from sperm chromatin after fertilization.