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首页> 外文期刊>Journal of Molecular Biology >Interaction surface of the transcription terminator Rho required to form a complex with the C-terminal domain of the antiterminator NusG.
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Interaction surface of the transcription terminator Rho required to form a complex with the C-terminal domain of the antiterminator NusG.

机译：转录终止子Rho的相互作用表面需要与抗终止子NusG的C端结构域形成复合物。

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摘要

Rho-dependent transcription termination in bacteria requires an interaction between the terminator Rho and the antiterminator NusG. The interaction surface of the Rho-NusG complex is unknown. Here we provide direct evidence that the beta-sheet bundle of the C-terminal domain of NusG (NusG-CTD) has the binding determinants for Rho, proving the hypothesis described earlier [Mooney, R. A., Schweimer, K., Rosch, P., Gottesman, M., & Landick, R., (2009). Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J. Mol. Biol., 391, 341-358.]. Disulfide bridges can be engineered from NusG-CTD with the surface-exposed amino acids 217 and 224 of Rho, which belong to its P-loop ATPase domain. Mutational analyses of this region of Rho revealed that a hydrophobic pocket, located behind these amino acids of Rho, is the docking site for NusG-CTD. The proximity of this region of Rho to NusG-CTD in the Rho-NusG complex was also confirmed by an efficient fluorescence resonance energy transfer between residue K224 of Rho and residue A168 of NusG-CTD. The identification of the Rho-NusG interaction surface will be useful not only in understanding the role of NusG in the termination process but also in explaining the molecular basis of the involvement of NusG-CTD in recruiting Rho and the ribosome to the same transcription machinery.
机译：细菌中依赖Rho的转录终止需要终止子Rho和抗终止子NusG之间的相互作用。 Rho-NusG复合物的相互作用表面是未知的。在这里，我们提供了直接的证据，即NusG（NusG-CTD）C端结构域的β-折叠束具有Rho的结合决定簇，证明了先前描述的假设[Mooney，RA，Schweimer，K.，Rosch，P. ，Gottesman，M.和Randick，R.（2009）。大肠杆菌NusG的两个结构独立的结构域通过与RNA聚合酶和调节剂的独特相互作用而产生了调节可塑性。 J.摩尔生物化学杂志，391，341-358。可以从NusG-CTD中利用Rho的表面暴露氨基酸217和224设计二硫键，这些氨基酸属于其P环ATPase结构域。对Rho区域的突变分析表明，位于Rho这些氨基酸后面的疏水口袋是NusG-CTD的停靠位点。 Rho-NusG复合物中Rho的这一区域与NusG-CTD的接近也通过Rho残基K224和NusG-CTD残基A168之间有效的荧光共振能量转移得以证实。 Rho-NusG相互作用表面的鉴定将不仅有助于理解NusG在终止过程中的作用，而且有助于解释NusG-CTD在将Rho和核糖体募集到同一转录机制中的分子基础。

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