A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription.
A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription.
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激酶缺陷的转录因子 TFIIH 在基础转录和激活转录中发挥作用。
DOI：
10.1073/pnas.92.11.5174
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发表时间：
1995
影响因子：
11.1
通讯作者：
Weinberg,RA
中科院分区：
文献类型：
--
作者：
Mäkelä,TP;Parvin,JD;Kim,J;Huber,LJ;Sharp,PA;Weinberg,RA
RNA聚合酶II大亚基的羧基末端结构域（CTD）的磷酸化被认为是转录起始、激活或延伸的关键。CTD特异性激酶活性是一般转录因子TFIIH的组分。最近，发现一种细胞周期蛋白依赖性激酶激活剂激酶（MO15和细胞周期蛋白H）与TFIIH制剂相关，并被认为是CTD激酶。TFIIH制剂含有突变体，激酶缺陷型MO15缺乏CTD激酶活性，表明MO15对聚合酶磷酸化至关重要。尽管如此，这些突变TFIIH制剂在基础和活化转录中都是完全功能性的（体外）。这些结果表明，CTD磷酸化是不需要的转录与高度纯化的系统。
Phosphorylation of the carboxyl-terminal domain (CTD) of the large subunit of RNA polymerase II has been suggested to be critical for transcription initiation, activation, or elongation. A kinase activity specific for CTD is a component of the general transcription factor TFIIH. Recently, a cyclin-dependent kinase-activator kinase (MO15 and cyclin H) was found to be associated with TFIIH preparations and was suggested to be the CTD kinase. TFIIH preparations containing mutant, kinase-deficient MO15 lack CTD kinase activity, indicating that MO15 is critical for polymerase phosphorylation. Nonetheless, these mutant TFIIH preparations were fully functional (in vitro) in both basal and activated transcription. These results indicate that CTD phosphorylation is not required for transcription with a highly purified system.