雌激素受体与组蛋白相互作用的评估。
Assessment of estrogen receptor--histone interactions.
作者信息
Kallos J, Fasy T M, Hollander V P
出版信息
Proc Natl Acad Sci U S A. 1981 May;78(5):2874-8. doi: 10.1073/pnas.78.5.2874.
Several different in vitro binding assays show that the estrogen receptor from rabbit uterus interacts selectively with purified histones from calf thymus. The estrogen receptor binds strongly to histones H2B and H2A, moderately to histones H3 and H4, and poorly to histone H1. In the presence of histones H2B or H2A, the position at which the estrogen receptor focuses in an isoelectric gradient is shifted to a more basic zone. Kinetic experiments show that, if histone H2B is bound to a DNA, the estrogen receptor dissociates more slowly from that DNA. The portion of the estrogen receptor molecule required for binding to histone H2B is relatively stable to tryptic digestion; in contrast, the portion of the receptor molecule responsible for DNA binding is promptly lost during limited tryptic digestion. These in vitro findings suggest that the mechanism by which the estrogen receptor selectively alters gene expression may involve specific contacts with histone molecules.
几种不同的体外结合试验表明，兔子宫中的雌激素受体与小牛胸腺纯化的组蛋白选择性相互作用。雌激素受体与组蛋白H2B和H2A强烈结合，与组蛋白H3和H4中度结合，与组蛋白H1结合较弱。在存在组蛋白H2B或H2A的情况下，雌激素受体在等电梯度中聚焦的位置会向更碱性的区域移动。动力学实验表明，如果组蛋白H2B与DNA结合，雌激素受体从该DNA上解离得更慢。与组蛋白H2B结合所需的雌激素受体分子部分对胰蛋白酶消化相对稳定；相比之下，负责DNA结合的受体分子部分在有限的胰蛋白酶消化过程中会迅速丢失。这些体外研究结果表明，雌激素受体选择性改变基因表达的机制可能涉及与组蛋白分子的特异性接触。
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