Palau J, Climent F, Avilés F J, Morros A, Soliva M
Biochim Biophys Acta. 1977 May 17;476(2):108-21. doi: 10.1016/0005-2787(77)90088-0.
The interactions of DNA with the five histone components (H1, H2B, H2A, H3 and H4) and with a number of histone fragments (N-H1 (1--72), C-H1 (73--216), N-H2B (l--59), C-H2B, (63--125), N-H2A (1-39), C-H2A (58--129), N-H4 (1--84) and C-H4 (85--102) have been studied by using the techniques of thermal denaturation and solubility behaviour. Complexes in 10(-3) M phosphate buffer, 2 - 10(-5) M Na(2)-EDTA, pH 7.0 were prepared by the direct mixing method. For lysine-rich histones (H1 and H2B) it has been found that the main characteristics which governs the interaction with DNA are located in the very lysine-rich part of the molecules, i.e. in the C-H1 and N-H2B segments. These regions are also responsible for a cooperative distribution of the histone along the DNA molecules in the artificial complexes. It appears from our studies that the tertiary structure of the moderately, arginine-rich histone (H2A) is an essential feature for its interaction with DNA. The two arginine-rich histones (H3 and H4) complexed with DNA behave in a similar way, both in thermal denaturation and in DNA precipitation. In the case of C-H4, a marked shift of the melting profile has been observed which is correlated with the presence in the peptide of the hydrophilic cluster Lys-Arg-Gln-Gly-Arg-Thr. Our results suggest that large segments rich in lysine and basic clustering within histones give rise to different modes of electrostatic interaction with DNA.
通过热变性技术和溶解性研究了DNA与五种组蛋白成分（H1、H2B、H2A、H3和H4）以及一些组蛋白片段（N - H1（1 - 72）、C - H1（73 - 216）、N - H2B（1 - 59）、C - H2B（63 - 125）、N - H2A（1 - 39）、C - H2A（58 - 129）、N - H4（1 - 84）和C - H4（85 - 102））之间的相互作用。采用直接混合法在10⁻³ M磷酸盐缓冲液、2 - 10⁻⁵ M Na₂ - EDTA、pH 7.0条件下制备复合物。对于富含赖氨酸的组蛋白（H1和H2B），已发现决定其与DNA相互作用的主要特征位于分子中富含赖氨酸的部分，即C - H1和N - H2B片段。这些区域还负责在人工复合物中组蛋白沿DNA分子的协同分布。我们的研究表明，中等富含精氨酸的组蛋白（H2A）的三级结构是其与DNA相互作用的一个基本特征。与DNA复合的两种富含精氨酸的组蛋白（H3和H4）在热变性和DNA沉淀方面表现相似。在C - H4的情况下，观察到熔解曲线有明显偏移，这与肽中亲水簇Lys - Arg - Gln - Gly - Arg - Thr的存在相关。我们的结果表明，组蛋白中富含赖氨酸的大片段和碱性簇会导致与DNA不同的静电相互作用模式。
