Ramm E I, Chikhirzhina E V, Kostyleva E N, Vorob'ev V I
Biokhimiia. 1995 Jan;60(1):150-8.
A comparison of conformational potencies of linker histones of the H1 family has been performed by the curcular dichroism (CD) method. The histones were isolated from sera urchin (Strongylocentrotus intermedius), starfish (Aphelasterias japonica) and mollusc (Chlamis islandicus) sperm and rat thymus. The presence of an additional alpha-helical segment in the C-terminal part of the H1 histone from sea urchin sperm has been found to be a characteristic peculiarity of echinoderm sperm linker histones H1. The conformational properties of the H1 from starfish and sea urchin sperm are similar. The terminal domain of the mollusc sperm H1 has a more stable conformation of the left-handed helix in comparison with histones H1 of a different origin. It has been shown that the terminal fragments of the tested histones play an essential role in thermal stabilization of the secondary and ternary structures of the globular domains in these histones. The results obtained point to the difference in the mechanisms of supercondensed organization of sperm chromatin. The role of H1 histones in this process is discussed.
已通过圆二色性（CD）方法对H1家族连接组蛋白的构象活性进行了比较。这些组蛋白从海胆（中间球海胆）、海星（日本海燕）、软体动物（冰岛丽蚌）精子以及大鼠胸腺中分离得到。已发现海胆精子H1组蛋白C末端部分存在一个额外的α螺旋片段，这是棘皮动物精子连接组蛋白H1的一个特征性特性。海星和海胆精子H1的构象性质相似。与不同来源的H1组蛋白相比，软体动物精子H1的末端结构域具有更稳定的左手螺旋构象。结果表明，所测试组蛋白的末端片段在这些组蛋白球状结构域二级和三级结构的热稳定中起着重要作用。所得结果表明精子染色质超浓缩组织机制存在差异。文中讨论了H1组蛋白在此过程中的作用。
