Structural basis of transcription activation.
Structural basis of transcription activation.
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DOI：
10.1126/science.aaf4417
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发表时间：
2016-06-10
期刊：
影响因子：
--
通讯作者：
Ebright RH
中科院分区：
文献类型：
--
作者：
Feng Y;Zhang Y;Ebright RH
II类转录激活因子通过结合与核心启动子重叠的DNA位点并刺激初始RNA聚合酶（RNAP）-启动子封闭复合物异构化为催化活性RNAP-启动子开放复合物来发挥作用。在这里，我们报告了一个完整的细菌II类转录激活复合物的4.4 μ m晶体结构。其结构包括嗜热栖热菌转录激活蛋白TTHB 099（TAP;大肠杆菌分解代谢物激活蛋白CAP的同源物）、嗜热栖热菌转录激活蛋白TTHB 099（TAP;大肠杆菌分解代谢物激活蛋白CAP的同源物）、嗜热栖热菌转录激活蛋白TTHB 099（TAP;大肠杆菌分解代谢物激活蛋白CAP的同源物）。嗜热菌RNAP σA全酶、II类TAP依赖性启动子和核糖四核苷酸引物。该结构揭示了RNAP全酶与负责转录起始的DNA之间的相互作用，并揭示了TAP与负责转录激活的RNAP全酶之间的相互作用。结构表明TAP通过与RNAP全酶的简单、粘附、稳定的蛋白质-蛋白质相互作用刺激异构化。
Class II transcription activators function by binding to a DNA site overlapping a core promoter and stimulating isomerization of an initial RNA polymerase (RNAP)-promoter closed complex into a catalytically competent RNAP-promoter open complex. Here we report a 4.4 Å crystal structure of an intact bacterial Class II transcription activation complex. The structure comprises Thermus thermophilus transcription activator protein TTHB099 (TAP; homolog of Escherichia coli catabolite activator protein, CAP), T. thermophilus RNAP σA holoenzyme, a Class II TAP-dependent promoter, and a ribotetranucleotide primer. The structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription initiation and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation. The structure indicates that TAP stimulates isomerization through simple, adhesive, stabilizing protein-protein interactions with RNAP holoenzyme.