Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.
Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.
复制标题
DOI：
10.1016/s0006-3495(98)77990-1
复制
发表时间：
1998-06
影响因子：
3.4
通讯作者：
S. Leuba;Carlos Bustamante;Carlos Bustamante;K. Holde;Jordanka J. Zlatanova;Jordanka J. Zlatanova
中科院分区：
文献类型：
--
作者：
S. Leuba;Carlos Bustamante;Carlos Bustamante;K. Holde;Jordanka J. Zlatanova;Jordanka J. Zlatanova
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。在一篇同伴论文(Leuba， S. H.等。1998.生物物理学报。74:2823-2829)，我们通过对轻度胰蛋白酶化纤维的扫描力显微镜成像，研究了连接子组蛋白结构域和核心组蛋白H3的n端尾部对延长染色质纤维结构的贡献。在这里，我们通过选择性重建的染色质纤维的扫描力显微镜成像来补充和扩展这些研究，这些纤维在其组蛋白组成方面存在细微但独特的差异。我们证明了在确定构象稳定性时，对连接组蛋白的球形结构域和连接组蛋白尾部和组蛋白H3的结构冗余的绝对要求。
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.