CHROMATIN SUPERSTRUCTURE - A STUDY WITH AN IMMOBILIZED TRYPSIN
CHROMATIN SUPERSTRUCTURE - A STUDY WITH AN IMMOBILIZED TRYPSIN
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DOI：
10.1016/0014-5793(86)81161-9
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发表时间：
1986-05-12
期刊：
影响因子：
3.5
通讯作者：
PASHEV, IG
中科院分区：
文献类型：
--
作者：
DIMITROV, SI;APOSTOLOVA, TM;PASHEV, IG
用固定于胶原膜上的胰蛋白酶处理Hen红细胞染色质，染色质纤维展开后进行90°光散射和流动线性二色。当大部分H1和H5被消化而H3仍然完整时，发现染色质几乎完全去致密。进一步消化导致H3和其余H1和H5的降解不超过总效应的10-15%。当用增加亚精胺量的方法滴定胰蛋白酶切割的H1和H5染色质时，其折叠方式与对照样品相似。这一发现表明，电荷中和可能是通过H1和H5的c端结构域维持30 nm染色质纤维结构的一种机制。
Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10–15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.