染色质连接蛋白 HMGB1 和 H1 及其复合物的二级结构分析

IF 4.033 Q4 Biochemistry, Genetics and Molecular Biology Biophysics Pub Date : 2024-03-07 DOI:10.1134/S0006350923050081

E. V. Chikhirzhina, A. M. Polyanichko

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引用次数: 0

摘要

摘要非组蛋白染色体蛋白HMGB1和组蛋白H1是染色质连接蛋白。连接蛋白的功能与其构象状态密切相关。在染色质高级结构组织形成过程中起关键作用的蛋白质的结构正在被积极研究。本研究对连接蛋白组蛋白 H1 和非组蛋白 HMGB1 的二级结构进行了比较分析。利用紫外区的圆二色性和傅立叶变换红外光谱，研究表明，带正电荷的组蛋白 H1 与 HMGB1 的 C 端片段结合，稳定了由此产生的复合物，并促使两种蛋白质形成额外的 α 螺旋区域。

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Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes

The nonhistone chromosomal protein HMGB1 and histone H1 are chromatin linker proteins. The functions of linker proteins are closely related to their conformational state. The structure of proteins that play a key role in the formation of higher levels of chromatin structural organization is being actively studied. In this study, a comparative analysis of the secondary structure of the linker histone H1 and the nonhistone protein HMGB1 was carried out. Using circular dichroism in the UV region and FTIR spectroscopy, it was shown that positively charged histone H1 binds to the C-terminal fragment of HMGB1, stabilizing the resulting complex and inducing the formation of additional α-helical regions in both proteins.

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来源期刊

Biophysics Biochemistry, Genetics and Molecular Biology-Biophysics

CiteScore

1.20

自引率

0.00%

发文量

期刊介绍： Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.