Graziano V, Gerchman S E, Schneider D K, Ramakrishnan V
Biology Department, Brookhaven National Laboratory, Upton, New York 11973.
Nature. 1994 Mar 24;368(6469):351-4. doi: 10.1038/368351a0.
The linker histone H1 binds to the nucleosome and is essential for the organization of nucleosomes into the 30-nm filament of chromatin. It has been implicated in the repression of transcription, and phosphorylation of H1 may be involved in cell-cycle-dependent chromatin condensation and decondensation. A long-standing issue concerns the location of H1 in the chromatin filament. The original solenoidal model proposes that H1 is inside the 30-nm filament, but other models, also helical, suggest a variable or more accessible location for H1. Investigations to determine the location of the linker histone based on its accessibility to antibodies or immobilized proteases under various ionic conditions have yielded conflicting results. Here we use neutron scattering in a direct structural determination to show that H1 is located in the interior of the filament.
连接组蛋白H1与核小体结合,对于将核小体组织成30纳米染色质细丝至关重要。它与转录抑制有关,H1的磷酸化可能参与细胞周期依赖性染色质的凝聚和解聚。一个长期存在的问题是H1在染色质细丝中的位置。最初的螺线管模型提出H1在30纳米细丝内部,但其他同样呈螺旋状的模型则表明H1的位置可变或更容易接近。基于在各种离子条件下连接组蛋白对抗体或固定化蛋白酶的可及性来确定其位置的研究得出了相互矛盾的结果。在这里,我们通过直接结构测定使用中子散射来表明H1位于细丝内部。