Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities
Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcription activities
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DOI：
10.1074/jbc.m002578200
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发表时间：
2000-07-28
影响因子：
4.8
通讯作者：
Egly, JM
中科院分区：
文献类型：
--
作者：
Busso, D;Keriel, A;Egly, JM
转录/DNA修复因子TFIIM可以分解为至少两个亚复合物：核心TFIIH和cdk激活激酶（CAR）复合物。CAK复合物也在细胞中游离存在，由cdk 7、细胞周期蛋白H和MAT 1组成。在本工作中，我们发现MAT 1的C末端与cdk 7细胞周期蛋白II复合物结合并激活cdk 7激酶活性。MAT 1的中间部分含有卷曲螺旋基序，允许CAK通过与XPD和XPB解旋酶的相互作用结合到TFIIH核心。此外，使用重组TFIIH复合物，证明了MAT 1的N-末端RING指结构域对于转录激活是至关重要的，并且参与RNA聚合酶II的最大亚基的C-末端结构域的磷酸化。
The transcription/DNA repair factor TFIIM may be resolved into at least two subcomplexes: the core TFIIH and the cdk-activating kinase (CAR) complex. The CAK complex, which is also found free in the cell, is composed of cdk7, cyclin H, and MAT1. In the present work, we found that the C terminus of MAT1 binds to the cdk7 cyclin Ii complex and activates the cdk7 kinase activity. The median portion of MAT1, which contains a coiled-coil motif, allows the binding of CAK to the TFIIH core through interactions with both XPD and XPB helicases. Furthermore, using recombinant TFIIH complexes, it is demonstrated that the N-terminal RING finger domain of MAT1 is crucial for transcription activation and participates to the phosphorylation of the C-terminal domain of the largest subunit of the RNA polymerase II.