Roark D E, Geoghegan T E, Keller G H, Matter K V, Engle R L
Biochemistry. 1976 Jul 13;15(14):3019-25. doi: 10.1021/bi00659a013.
Histone interactions in solution may depend upon treatments used for purification. Optical rotatory dispersion and sedimentation-velocity measurements have been made in a reference solvent, before and after exposure to various treatments, to investigate histone susceptibility to irreversible denaturation. Some acid conditions and urea and guanidine solutions may denature. Interaction studies performed on nondenatured histones indicate that the dimer, (H4)(H3), and tetramer, (H4)2(H3)2, dissociate to monomers at low ionic strength. Sedimentation-velocity experiments suggest a model for the (H4)2(H3)2 tetramer, with a compact semispherical center and four protruding amino-terminal regions. Fractions H2a and H2b interact to form the mixed dimer in equilibrium with monomers. Fraction H2a self-associates readily to dimers, tetramers, and octamers, while fraction H1 associates only weakly to form dimers.
溶液中的组蛋白相互作用可能取决于用于纯化的处理方法。在暴露于各种处理之前和之后,已在参考溶剂中进行了旋光色散和沉降速度测量,以研究组蛋白对不可逆变性的敏感性。某些酸性条件以及尿素和胍溶液可能会使其变性。对未变性组蛋白进行的相互作用研究表明,二聚体(H4)(H3)和四聚体(H4)2(H3)2在低离子强度下会解离为单体。沉降速度实验提出了一个(H4)2(H3)2四聚体的模型,其具有紧密的半球形中心和四个突出的氨基末端区域。H2a和H2b组分相互作用形成与单体处于平衡状态的混合二聚体。H2a组分很容易自缔合形成二聚体、四聚体和八聚体,而H1组分仅弱缔合形成二聚体。