Allan J, Mitchell T, Harborne N, Bohm L, Crane-Robinson C
J Mol Biol. 1986 Feb 20;187(4):591-601. doi: 10.1016/0022-2836(86)90337-2.
Peptides derived from calf thymus H1 and rat liver H1, comprising only the globular and COOH-terminal domains of the intact molecule and therefore lacking NH2-terminal domains, have been shown by reconstitution to be as effective as the complete H1 molecule in inducing higher-order-chromatin structure. As the globular domain of H1 alone cannot induce chromatin folding, our results demonstrate that this function is primarily controlled by the COOH-terminal domain of the molecule. Surprisingly, these peptides do not locate correctly with respect to the nucleosome. This is demonstrated by their failure to confer upon reconstitutes the ability to protect DNA fragments of chromatosome length when digested with micrococcal nuclease. The precise placement of the H1 molecule (globular domain) with respect to the nucleosome is shown to be influenced by the "tail" domains of both H1 and the core histones.
从小牛胸腺H1和大鼠肝脏H1衍生而来的肽段，仅包含完整分子的球状结构域和COOH末端结构域，因此缺少NH2末端结构域。通过重组实验表明，这些肽段在诱导高阶染色质结构方面与完整的H1分子一样有效。由于单独的H1球状结构域不能诱导染色质折叠，我们的结果表明，该功能主要由分子的COOH末端结构域控制。令人惊讶的是，这些肽段在核小体上的定位不正确。这通过以下事实得到证明：当用微球菌核酸酶消化时，它们无法赋予重组体保护染色质体长度的DNA片段的能力。结果表明，H1分子（球状结构域）相对于核小体的精确位置受H1和核心组蛋白的“尾部”结构域的影响。
