Molecular structure of human TFIIH
Molecular structure of human TFIIH
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DOI：
10.1016/s0092-8674(00)00082-9
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发表时间：
2000-09-01
期刊：
影响因子：
64.5
通讯作者：
Egly, JM
中科院分区：
文献类型：
--
作者：
Schultz, P;Fribourg, S;Egly, JM
TFIIH 是转录和 DNA 修复所需的多蛋白复合物。通过电子显微镜和图像处理以 3.8 nm 的分辨率显示了人类 TFIIH 的单颗粒。 TFIIH 大小为 16 x 12.5 x 7.5 nm，组织成环状结构，其中突出有一个大的蛋白质结构域。由五个重组核心亚基组装而成的子复合物也形成圆形结构，可以叠加在人 TFIIH 中发现的环上。免疫标记实验定位了几个亚基：p44，在环状结构内，形成突出蛋白质密度的基础，其中包括 cdk7 激酶、细胞周期蛋白 H 和 MAT1。在环结构内，p44 的两侧分别是 XPB 和 XPD 解旋酶。这些观察结果为我们提供了 TFIIH 的四元组织模型。
TFIIH is a multiprotein complex required for both transcription and DNA repair. Single particles of human TFIIH were revealed by electron microscopy and image processing at a resolution of 3.8 nm. TFIIH is 16 x 12.5 x 7.5 nm in size and is organized into a ring-like structure from which a large protein domain protrudes out. A subcomplex assembled from five recombinant core subunits also forms a circular architecture that can be superimposed on the ring found in human TFIIH. Immunolabeling experiments localize several subunits: p44, within the ring structure, forms the base of the protruding protein density which includes the cdk7 kinase, cyclin H, and MAT1. Within the ring structure, p44 was flanked on either side by the XPB and XPD helicases. These observations provide us with a quartenary organizational model of TFIIH.