离子强度诱导的组蛋白H4及其片段的结构

Ionic strength induced structure in histone H4 and its fragments.

作者信息

Lewis P N, Bradbury M, Crane-Robinson C

出版信息

Biochemistry. 1975 Jul 29;14(15):3391-400. doi: 10.1021/bi00686a016.

Abstract

The salt-induced folding and self-association of histone H4 and its fragments (1-23), (25-67), (69-84), and (69-102) have been studied at the same molar concentration (1 mM) by nuclear magnetic resonance (NMR), circular dichroism (CD), and ir spectroscopy. Byeach of these techniques intact histone H4 exhibited a fast structural change, involving the formation of alphaR helix and aggregation, and also a slow change involving beta-structure formation. Fragment (25-67) was found to behave in a manner similar to the intact molecule for the fast change, showing both helix formation and aggregation but exhibited no time-dependent effects. All the other fragments were found to be essentially noninteracting. It is concluded that (25-67) contains the rgion critical for the folding and self-association of histone H4. On the basis of these results a model is proposed for the self-association of histone H4 in which helix is located between residues 49 and 73, while the beta structure lies between 74 and the C-terminus.

摘要

通过核磁共振（NMR）、圆二色性（CD）和红外光谱，在相同摩尔浓度（1 mM）下研究了盐诱导的组蛋白H4及其片段（1 - 23）、（25 - 67）、（69 - 84）和（69 - 102）的折叠和自缔合。通过这些技术中的每一种，完整的组蛋白H4都表现出快速的结构变化，包括αR螺旋的形成和聚集，以及涉及β结构形成的缓慢变化。发现片段（25 - 67）在快速变化方面的行为与完整分子相似，既显示出螺旋形成又有聚集，但没有时间依赖性效应。发现所有其他片段基本上不相互作用。得出的结论是，（25 - 67）包含对组蛋白H4折叠和自缔合至关重要的区域。基于这些结果，提出了一个组蛋白H4自缔合的模型，其中螺旋位于49至73位残基之间，而β结构位于74位至C末端之间。