Genest D, Sabeur G, Wahl P, Aubel-Sadron G
Biophys Chem. 1981 Feb;13(1):89-96. doi: 10.1016/0301-4622(81)80028-2.
The influence of H1 and H5 histones proteins upon the accessibility of ethidium bromide into chromatin is studied by steady-state fluorescence anisotropy in the range of r-values ([Dye]/[Phosphate]) smaller than 0.01. This corresponds to the very strong binding process. When H1 and H5 are present, the DNA segment which contains the binding sites is 25-30 base pairs long, even if H1 and H5 are digested by trypsin or by natural proteolysis, but presumably still interacting with the DNA chromatin. On the contrary, when H1 or H5 are separated from chromatin by an increase of the ionic strength, ethidium binds to a segment of DNA about 55-60 base pairs long. We may explain the results by assuming that the ethidium sites are located on a continuous segment constituting about one half of the linker, the other half interacting with H1 and H5. When chromatin is depleted from these proteins, the high affinity sites are distributed all along the linker.
通过稳态荧光各向异性研究了H1和H5组蛋白对溴化乙锭进入染色质的可及性的影响，研究范围为r值（[染料]/[磷酸盐]）小于0.01。这对应于非常强的结合过程。当存在H1和H5时，即使H1和H5被胰蛋白酶或自然蛋白酶消化，但可能仍与DNA染色质相互作用，含有结合位点的DNA片段长度为25 - 30个碱基对。相反，当通过增加离子强度将H1或H5与染色质分离时，溴化乙锭会结合到一段约55 - 60个碱基对长的DNA片段上。我们可以通过假设溴化乙锭位点位于构成连接体约一半的连续片段上来解释这些结果，连接体的另一半与H1和H5相互作用。当这些蛋白质从染色质中耗尽时，高亲和力位点沿连接体分布。
