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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >New insights into the membrane association mechanism of the glycosyltransferase WaaG from Escherichia coli
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New insights into the membrane association mechanism of the glycosyltransferase WaaG from Escherichia coli

机译：来自大肠杆菌糖基转移酶滑动糖基转移酶滑动的新见解

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摘要

Monotopic glycosyltransferases (GTs) interact with membranes via electrostatic interactions. The N-terminal domain is permanently anchored to the membrane while the membrane interaction of the C-terminal domain is believed to be weaker so that it undergoes a functionally relevant conformational change upon donor or acceptor binding. Here, we studied the applicability of this model to the glycosyltransferase WaaG. WaaG is involved in the synthesis of lipopolysaccharides (LPS) in Gram-negative bacteria and was previously categorized as a monotopic GT. We analyzed the binding of WaaG to membranes by stopped-flow fluorescence and NMR diffusion experiments. We find that electrostatic interactions are required to bind WaaG to membranes while mere hydrophobic interactions are not sufficient. WaaG senses the membrane's surface charge density but there is no preferential binding to specific anionic lipids. However, the binding is weaker than expected for monotopic GTs but similar to peripheral GTs. Therefore, WaaG may be a peripheral GT and this could be of functional relevance in vivo since LPS synthesis occurs only when WaaG is membrane-bound. We could not observe a C-terminal domain movement under our experimental conditions.
机译：单色糖基转移酶（GTS）通过静电相互作用与膜相互作用。 N-末端结构域永久地固定在膜上，同时C-末端结构域的膜相互作用较弱，使得其在供体或受体结合时经历功能相关的构象变化。在这里，我们研究了该模型的适用性至糖基转移酶的曲折。 WAAG参与革兰氏阴性细菌的脂多糖（LPS）的合成，并以先前分类为单位外GT。我们通过停止流动荧光和NMR扩散实验分析了WAAG对膜的结合。我们发现需要静电相互作用来对膜结合到膜上，而疏水性相互作用是不够的。 WAAG感测膜的表面电荷密度，但没有优先结合特异性阴离子脂质。然而，联合的结合比单表GTS的预期弱，而是与外周GTS类似。因此，WAAG可以是外周GT，并且这可以是体内功能相关性，因为只有在WAAG是膜结合时才发生LPS合成。在我们的实验条件下，我们无法观察到C终端域运动。

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