RNAP subunits F/E (RPB4/7) are stably associated with archaeal RNA polymerase: using fluorescence anisotropy to monitor RNAP assembly in vitro
RNAP subunits F/E (RPB4/7) are stably associated with archaeal RNA polymerase: using fluorescence anisotropy to monitor RNAP assembly in vitro
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DOI：
10.1042/bj20090782
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发表时间：
2009-08-01
影响因子：
4.1
通讯作者：
Werner, Finn
中科院分区：
文献类型：
--
作者：
Grohmann, Dina;Hirtreiter, Angela;Werner, Finn
细胞和真核生物RNAP（DNA依赖性RNA聚合酶）是复杂的多亚基酶。其中两个亚基，F和E，共同形成F/E复合物，已被假设在转录周期中以可逆的方式与RNAP结合。我们已经表征了F/E复合物和RNAP核心之间的分子相互作用。F/E以亚微摩尔亲和力与RNAP结合，并且不与未结合的F/E进行动态交换。
Archaeal and eukaryotic RNAPs (DNA-dependent RNA polymerases) are complex multi-subunit enzymes. Two of the subunits, F and E, which together form the F/E complex, have been hypothesized to associate with RNAP in a reversible manner during the transcription cycle. We have characterized the molecular interactions between the F/E complex and the RNAP core. F/E binds to RNAP with submicromolar affinity and is not in a dynamic exchange with unbound F/E.