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溶液中核心组蛋白的八聚体:H3-H4四聚体在自组装中的核心作用。

An octamer of core histones in solution: central role of the H3-H4 tetramer in the self-assembly.

作者信息

Ruiz-Carrillo A, Jorcano J L

出版信息

Biochemistry. 1979 Mar 6;18(5):760-8. doi: 10.1021/bi00572a004.

Abstract

The association of histones H2A, H2B, H3, and H4 in solution has been studied. In 2 M NaCl and at neutral pH they can assemble in a complex in which each histone is present in equimolar amounts. The complex has a weight average molecular weight of 98,000 (+/- 3700) and a sedimentation coefficient (so20,w) of 4.8. The value of the weight average molecular weight and the histone stoichiometry indicate that the complex is an octamer. The pairs of histones H2A,H2B and H3,H4 studied separately under identical conditions only associated as equimolar complexes consistent with dimeric and tetrameric structures, respectively. The stability of the core histone octamer is a function of the ionic strength, pH, and concentration of protein. The octamer dissociates by losing dimers of H2A,H2B until the main complexes existing in solution are the H3.H4 tetramer and the H2A.H2B dimer. This process is reversible upon reestablishing the original conditions.

摘要

已经对溶液中组蛋白H2A、H2B、H3和H4的缔合进行了研究。在2M氯化钠和中性pH条件下,它们可以组装成一种复合物,其中每种组蛋白以等摩尔量存在。该复合物的重均分子量为98,000(±3700),沉降系数(s20,w)为4.8。重均分子量的值和组蛋白化学计量表明该复合物是一个八聚体。在相同条件下分别研究的组蛋白对H2A、H2B和H3、H4仅分别以与二聚体和四聚体结构一致的等摩尔复合物形式缔合。核心组蛋白八聚体的稳定性是离子强度、pH和蛋白质浓度的函数。八聚体通过失去H2A、H2B二聚体而解离,直到溶液中存在的主要复合物是H3.H4四聚体和H2A.H2B二聚体。在重新建立原始条件后,这个过程是可逆的。

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