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组蛋白尾巴与核心染色质的差异解离。

Differential dissociation of histone tails from core chromatin.

作者信息

Walker I O

出版信息

Biochemistry. 1984 Nov 6;23(23):5622-8. doi: 10.1021/bi00318a037.

Abstract

The dissociation of the trypsin-sensitive basic tails of the core histones in core chromatin has been followed as a function of [NaCl] using proton NMR spectroscopy. The tails dissociate in a highly cooperative all or none manner over the salt concentration range 0.2-0.6 M, that is, below the salt concentration required to dissociate the complete molecule. Assuming that each basic tail dissociates independently, the total number of salt linkages involved in binding the tails to DNA is 103. This equals the number of basic side chains in the tails of an octamer. The standard free energy of dissociation, delta G degree, in 1 M NaCl at 297 K is 3.6 kcal/mol. Temperature had no effect on the extent of dissociation up to 45 degrees C. However, between 45 and 65 degrees C, where the premelting transition in the core chromatin occurs, the tails dissociated completely. Dissociation of the tails was associated with a conformational transition in the DNA consistent with loss of supercoiling. From this, and the results of a previous study, it can be shown that the structured, trypsin-resistant domain of each core histone octamer makes 100 salt linkages to DNA. Thus, in 10 mM salt, each core octamer makes a total of 203 salt linkages to DNA.

摘要

利用质子核磁共振波谱法,研究了核心染色质中核心组蛋白的胰蛋白酶敏感碱性尾部的解离与[NaCl]浓度的关系。在0.2 - 0.6 M的盐浓度范围内,尾部以高度协同的全或无方式解离,即在解离整个分子所需的盐浓度以下。假设每个碱性尾部独立解离,将尾部与DNA结合所涉及的盐键总数为103。这等于一个八聚体尾部中碱性侧链的数量。在297 K的1 M NaCl中,解离的标准自由能ΔG°为3.6 kcal/mol。在45℃以下,温度对解离程度没有影响。然而,在45至65℃之间,核心染色质发生预熔转变,尾部完全解离。尾部的解离与DNA的构象转变有关,这与超螺旋的丧失一致。由此以及先前一项研究的结果可以表明,每个核心组蛋白八聚体的结构化、抗胰蛋白酶结构域与DNA形成100个盐键。因此,在10 mM盐中,每个核心八聚体与DNA总共形成203个盐键。

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