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首页> 外文期刊>Biochemistry >Phosphorylation Triggers Domain Separation in the DNA Binding Response Regulator NarL.
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Phosphorylation Triggers Domain Separation in the DNA Binding Response Regulator NarL.

机译：磷酸化触发DNA结合反应调节剂NarL中的结构域分离。

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摘要

DNA binding proteins of two-component signal transduction systems in microorganisms are activated by phosphorylation through an unknown mechanism. NarL is an example from the nitrateitrite signal transduction system of Eschericia coli. NarL consists of N- and C-terminal domains, the latter of which contains the DNA binding elements. To explore the mechanism of activation, single nitroxide side chains were introduced, one at a time, at nine different sites throughout the C-terminal domain to monitor the tertiary structure and the status of the surface in contact with the N-terminal domain. In addition, three pairs of doubly labeled proteins were prepared to monitor the interdomain distance using the magnetic dipolar interaction. The results of these site-directed spin-labeling studies reveal that phosphorylation at a distant site in the N-terminal domain triggers domain separation, likely by a hinge-bending motion. This in turn presents key elements of the C-terminal domain for docking to the DNA target in the configuration described in the recent crystal structure. The data also imply that a single conformation of unphosphorylated NarL exists in solution, and there is no detectable equilibrium between the closed and open conformations.
机译：微生物中两组分信号转导系统的DNA结合蛋白通过未知机制被磷酸化激活。 NarL是大肠杆菌硝酸盐/亚硝酸盐信号转导系统的一个实例。 NarL由N和C末端域组成，后者包含DNA结合元件。为了探索激活的机制，在整个C末端结构域的9个不同位点一次引入一条氮氧根侧链，以监测三级结构和与N末端结构域接触的表面状态。另外，使用磁偶极相互作用制备了三对双标记的蛋白质以监测域间距离。这些定点自旋标记研究的结果表明，N末端结构域远端位置的磷酸化可能触发结构域分离，这可能是由于铰链弯曲运动引起的。这继而呈现出以最近的晶体结构中所述的构型对接至DNA靶标的C端结构域的关键元件。该数据还暗示溶液中存在单一构象的未磷酸化的NarL，并且在闭合构象和开放构象之间没有可检测到的平衡。

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