Fisher R P, Jin P, Chamberlin H M, Morgan D O
Department of Physiology, University of California, San Francisco 94143-0444, USA.
Cell. 1995 Oct 6;83(1):47-57. doi: 10.1016/0092-8674(95)90233-3.
We have cloned a mouse cDNA that encodes p36, a novel subunit of the CDK-activating kinase (CAK). p36 contains a C3HC4 zinc-binding domain or RING factor and is associated both with a TFIIH-bound form of CAK and with a free trimeric form. p36 promotes the assembly of CDK7 and cyclin H in vitro, stabilizing the transient CDK7-cyclin H complex. Stabilization and activation of CAK by p36 is independent of the phosphorylation state of T170, the conserved activating residue of CDK7. Assembly of active CDK7-cyclin H dimers can also occur through an alternative p36-independent pathway that requires phosphorylation of T170 by a CAK-activating kinase, or CAKAK. Thus, CDK7-cyclin H complex formation can be achieved by multiple mechanisms.
我们克隆了一个小鼠cDNA，它编码p36，即细胞周期蛋白依赖性激酶激活激酶（CAK）的一个新亚基。p36含有一个C3HC4锌结合结构域或环状因子，并且与TFIIH结合形式的CAK以及游离三聚体形式都有关联。p36在体外促进CDK7和细胞周期蛋白H的组装，稳定瞬时的CDK7 - 细胞周期蛋白H复合物。p36对CAK的稳定和激活不依赖于T170的磷酸化状态，T170是CDK7保守的激活残基。活性CDK7 - 细胞周期蛋白H二聚体的组装也可以通过一条不依赖p36的替代途径发生，该途径需要一种CAK激活激酶（CAKAK）对T170进行磷酸化。因此，CDK7 - 细胞周期蛋白H复合物的形成可以通过多种机制实现。
