Suppr超能文献

[重组多核小体中组蛋白八聚体的结构]

[Structure of histone octamers in reconstituted polynucleosomes].

作者信息

Khrapunov S N, Sivolob A V, Dragan A I, Berdyshev G D

出版信息

Mol Biol (Mosk). 1985 Nov-Dec;19(6):1553-61.

PMID:4079932
Abstract

The salt-dependent structural changes of the histone octamer in complex with high-molecular-weight DNA have been studied by fluorescent spectroscopy. Changes in both the spectra maximum position and anisotropy of the histone tyrosine fluorescence reveal structural transitions in nucleosome within the ranges of 0.5-3 mM and 20-30 mM NaCl. Comparison of the octamer fluorescent parameters in complex with DNA as well as in a free state permits to interpret the revealed structural transitions as a change in degree of contacts stability between (H2A-H2B) dimer and (H3-H4)2 tetramer. More pronounced conformational changes in histone octamer are observed under the conditions of polynucleosome fibers interaction within the range of physiological ionic strength (100-600 mM NaCl). As far as fluorescent parameters are concerned, the aforementioned changes are connected with entire destruction of (H2A-H2B) dimer specific contacts with (H3-H4)2 tetramer. The obtained results suggest the possibility of existence of different structural states of histone octamer in the chromatin composition including those which are quite dissimilar from the octamer structure in the 2M NaCl solution.

摘要

通过荧光光谱法研究了与高分子量DNA复合的组蛋白八聚体的盐依赖性结构变化。组蛋白酪氨酸荧光的光谱最大位置和各向异性的变化揭示了在0.5 - 3 mM和20 - 30 mM NaCl范围内核小体中的结构转变。将与DNA复合以及处于游离状态的八聚体荧光参数进行比较,可以将所揭示的结构转变解释为(H2A - H2B)二聚体与(H3 - H4)2四聚体之间接触稳定性程度的变化。在生理离子强度范围(100 - 600 mM NaCl)内多聚核小体纤维相互作用的条件下,观察到组蛋白八聚体更明显的构象变化。就荧光参数而言,上述变化与(H2A - H2B)二聚体与(H3 - H4)2四聚体的特定接触的完全破坏有关。所得结果表明,在染色质组成中可能存在组蛋白八聚体的不同结构状态,包括那些与2M NaCl溶液中的八聚体结构非常不同的状态。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验