Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography
Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography
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DOI：
10.1016/j.jchromb.2013.04.003
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发表时间：
2013-06-15
影响因子：
3
通讯作者：
Li, Renqiang
中科院分区：
文献类型：
--
作者：
Cai, Hanning;Xie, Ying;Li, Renqiang
将从猪肝组织中纯化的组蛋白H2 a、H2 b、H3和H4固定在Sepharose 4 B上，制成组蛋白-Sepharose柱。在牛乳酪蛋白的组蛋白-琼脂糖凝胶层析过程中，发现组蛋白配体捕获了两种朊病毒蛋白（PrPc）亚型，分子量分别为34和30 kDa，分别对应于二糖基化和单糖基化PrPc。为了进一步验证组蛋白与PrPc之间的相互作用，制备了PrPc-Sepharose柱并用于分离组蛋白。两种层析方法和SOS-PAGE表明，只有组蛋白中的H3被发现与PrPc相互作用。本研究提示H3可能是PrPc在细胞核内的靶分子，这对了解朊病毒病有一定的意义。(C)2013 Elsevier B. V.保留所有权利。
The histones including H2a, H2b, H3 and H4 purified from pig liver tissue were immobilized onto Sepharose 4B to create a histone-Sepharose column. During chromatography of cow milk casein by histone-Sepharose column, two isoforms of prion protein (PrPc) with 34 and 30 kDa molecular mass corresponding to diglycosylated and monoglycosylated PrPc respectively were found to be captured by histone ligands. To further verify the interaction between histones and PrPc, the PrPc-Sepharose column was prepared and used to separate the histones. Two chromatography processes and SOS-PAGE demonstrated that only H3 in the histones was found to interact with PrPc. This study suggested H3 could be the target molecule of PrPc in nuclei, which might be useful for understanding the prion disease. (C) 2013 Elsevier B.V. All rights reserved.