连接组蛋白尾巴与组蛋白H3的N端尾巴功能冗余：重组纤维的扫描力显微镜研究
Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.
作者信息
Leuba S H, Bustamante C, van Holde K, Zlatanova J
机构信息
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
出版信息
Biophys J. 1998 Jun;74(6):2830-9. doi: 10.1016/S0006-3495(98)77990-1.
Abstract
The mechanisms responsible for organizing linear arrays of nucleosomes into the three-dimensional structure of chromatin are still largely unknown. In a companion paper (Leuba, S. H., et al. 1998. Biophys. J. 74:2823-2829), we study the contributions of linker histone domains and the N-terminal tail of core histone H3 to extended chromatin fiber structure by scanning force microscopy imaging of mildly trypsinized fibers. Here we complement and extend these studies by scanning force microscopy imaging of selectively reconstituted chromatin fibers, which differ in subtle but distinctive ways in their histone composition. We demonstrate an absolute requirement for the globular domain of the linker histones and a structural redundancy of the tails of linker histones and of histone H3 in determining conformational stability.
摘要
负责将核小体线性阵列组织成染色质三维结构的机制在很大程度上仍然未知。在一篇配套论文（Leuba, S. H.等人，1998年。《生物物理杂志》74:2823 - 2829）中，我们通过对轻度胰蛋白酶消化的纤维进行扫描力显微镜成像，研究了连接组蛋白结构域和核心组蛋白H3的N端尾巴对延伸染色质纤维结构的贡献。在这里，我们通过对选择性重构的染色质纤维进行扫描力显微镜成像来补充和扩展这些研究，这些纤维在组蛋白组成上存在细微但独特的差异。我们证明了连接组蛋白的球状结构域对于确定构象稳定性是绝对必需的，并且连接组蛋白和组蛋白H3的尾巴在结构上具有冗余性。
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