Role of the structural domains of linker histones and histone H3 in the chromatin fiber structure at low-ionic strength: scanning force microscopy (SFM) studies on partially trypsinized chromatin
Role of the structural domains of linker histones and histone H3 in the chromatin fiber structure at low-ionic strength: scanning force microscopy (SFM) studies on partially trypsinized chromatin
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低离子强度下连接组蛋白和组蛋白 H3 的结构域在染色质纤维结构中的作用：部分胰蛋白酶化染色质的扫描力显微镜 (SFM) 研究
DOI：
10.1117/12.205930
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
K. V. van Holde
中科院分区：
文献类型：
--
作者：
J. Zlatanova;S. Leuba;C. Bustamante;K. V. van Holde
用胰蛋白酶水解染色质纤维，用十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS PAGE）和扫描力显微镜（SFM）进行观察。在水解的早期点，当大多数只有连接组蛋白的尾部被切割时，核小体似乎在纤维内彼此堆积。之后，一旦组蛋白H3的N-末端尾部发生显著水解，纤维就表现出核小体的开放的三维排列。首次观察到相邻核小体之间的连接DNA。相邻的核小体似乎有一个“之字形”的安排。最后，当接头组蛋白的所有尾部和H3的N-末端尾部都被切割时，则纤维表现出（i）核小体的平坦二维排列，（ii）几乎所有核小体之间的接头DNA，和（iii）一些核小体之间的Z字形排列。我们认为：（i）连接子组蛋白球状结构域有助于固定DNA进入和离开核小体的角度，（ii）然而，该角度不足以维持纤维的三维性，以及（iii）组蛋白H3的N-末端尾部是低离子强度下纤维三维构象所必需的。
Chromatin fibers have been hydrolyzed by trypsin and examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) and scanning force microscopy (SFM). At early points of hydrolysis, when mostly only the tails of the linker histones have been cleaved, nucleosomes appear to pile upon each other within a fiber. Later, once significant hydrolysis of the N-terminal tail of histone H3 has occurred, fibers exhibit an open, three-dimensional arrangement of nucleosomes. Linker DNA between adjacent nucleosomes is observed for the first time. Adjacent nucleosomes appear to have a 'zig-zag' arrangement. Finally, when all the tails of the linker histones and the N-terminal tails of H3 have been cleaved, then the fibers exhibit (i) a flat two- dimensional arrangement of nucleosomes, (ii) linker DNA between nearly all nucleosomes, and (iii) a zig-zag arrangement among some nucleosomes. We suggest that (i) the linker histone globular domains help fix the angle of the DNA entering and exiting the nucleosome, (ii) the angle, however, is not sufficient to maintain the three-dimensionality of the fiber, and (iii) the N-terminal tails of histone H3 ares necessary for the three-dimensional conformation of the fiber at low ionic strength.
影响因子：
2.9
作者：
YAGER, TD;MCMURRAY, CT;VANHOLDE, KE
通讯作者：
VANHOLDE, KE