RNA聚合酶亚基F/E（RPB4/7）与古细菌RNA聚合酶稳定结合：利用荧光各向异性监测体外RNA聚合酶组装。
RNAP subunits F/E (RPB4/7) are stably associated with archaeal RNA polymerase: using fluorescence anisotropy to monitor RNAP assembly in vitro.
作者信息
Grohmann Dina, Hirtreiter Angela, Werner Finn
机构信息
Institute for Structural and Molecular Biology, Division of Biosciences, Darwin Building, University College London, Gower Street, London WC1E 6BT, UK.
出版信息
Biochem J. 2009 Jul 15;421(3):339-43. doi: 10.1042/BJ20090782.
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.
古菌和真核生物的RNA聚合酶（依赖DNA的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复合体，据推测在转录周期中它们与RNA聚合酶以可逆方式结合。我们已经对F/E复合体与RNA聚合酶核心之间的分子相互作用进行了表征。F/E以亚微摩尔亲和力与RNA聚合酶结合，并且不会与未结合的F/E进行动态交换。
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