A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor delta from rat liver.
A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor delta from rat liver.
复制标题
一种与大鼠肝脏 RNA 聚合酶 II 转录因子 δ 相关的羧基末端域激酶。
DOI：
10.1073/pnas.89.16.7476
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发表时间：
1992
影响因子：
11.1
通讯作者：
Conaway,JW
中科院分区：
文献类型：
--
作者：
Serizawa,H;Conaway,RC;Conaway,JW
We previously purified RNA polymerase II transcription factor delta from rat liver and found that it has an associated DNA-dependent ATPase (dATPase) activity. In this report, we show that delta is also closely associated with a protein kinase activity that catalyzes phosphorylation of the largest subunit of RNA polymerase II. Kinase activity copurifies with transcription and DNA-dependent ATPase (dATPase) activities when delta is analyzed by anion- and cation-exchange HPLC as well as by sucrose gradient sedimentation, arguing that delta possesses all three activities. Phosphorylation of the largest subunits of both rat and yeast RNA polymerase II is stimulated by DNA, whereas phosphorylation of a synthetic peptide containing multiple copies of the carboxyl-terminal heptapeptide repeat is not. Although both ATP and GTP appear to function as phosphate donors, GTP is utilized less than 10% as well as ATP. These findings suggest that delta may exert its action in transcription at least in part through a mechanism involving phosphorylation of the largest subunit of RNA polymerase II.
