果蝇的热休克蛋白与耐核酸酶、耐高盐的核结构相关。
Heat-shock proteins of Drosophila are associated with nuclease-resistant, high-salt-resistant nuclear structures.
作者信息
Levinger L, Varshavsky A
出版信息
J Cell Biol. 1981 Sep;90(3):793-6. doi: 10.1083/jcb.90.3.793.
Abstract
Proteins produced in cultured Drosophila cells during the heat-shock response (HSPs) were recently shown by autoradiography to be confined in large measure to the cell nucleus. We report here that nuclear HSPs are not associated with nucleosomes solubilizes by treatment with staphylococcal nuclease at low ionic strength nor are HSPs released by extraction with high salt, which solubilized most of the remaining histones and DNA. Possible functions of nuclear HSPs are discussed.
摘要
最近通过放射自显影法显示，在热休克反应（HSPs）期间培养的果蝇细胞中产生的蛋白质在很大程度上局限于细胞核。我们在此报告，核HSPs与在低离子强度下用葡萄球菌核酸酶处理而溶解的核小体不相关，并且HSPs也不会因用高盐提取而释放，高盐提取可溶解大部分剩余的组蛋白和DNA。文中讨论了核HSPs可能的功能。
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