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首页> 外文期刊>The FEBS journal >A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome
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A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome

机译：蛋白质结构的一个难题-探索由细菌植物色素设计的近红外荧光蛋白质iRFP

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The possibility of engineering near-infrared fluorescent proteins and biosensors from bacterial phytochrome photoreceptors (BphPs) has led to substantial interest in this family of proteins. The near-infrared fluorescent proteins have allowed non-invasive bio-imaging of deep tissues and whole organs in living animals. BphPs and derived near-infrared fluorescent proteins contain a structural element, called a knot, in their polypeptide chains. The formation of knot structures in proteins was refuted for a long time. Here, we studied the denaturation and renaturation processes of the near-infrared fluorescent probe iRFP, engineered from RpBphP2, which utilizes a heme-derived tetrapyrrole compound biliverdin as a chromophore. iRFP contains a unique figure-of-eight knot. The denaturation and renaturation curves of the iRFP apoform coincided well, suggesting efficient refolding. However, the iRFP holoform exhibited irreversible unfolding and aggregation associated with the bound chromophore. The knot structure in the apoform did not prevent subsequent binding of biliverdin, resulting in the functional iRFP holoform. We suggest that the irreversibility of protein unfolding is caused by post-translational protein modifications, such as chromophore binding, rather than the presence of the knot. These results are essential for future design of BphP-based near-infrared probes, and add important features to our knowledge of protein folding.
机译：从细菌植物色素光感受器（BphPs）工程近红外荧光蛋白和生物传感器的可能性已引起对该蛋白家族的极大兴趣。近红外荧光蛋白可以对动物的深部组织和整个器官进行非侵入性生物成像。 BphP和衍生的近红外荧光蛋白在其多肽链中包含一个称为结的结构元件。蛋白质中的结结构形成被长时间驳斥。在这里，我们研究了由RpBphP2设计的近红外荧光探针iRFP的变性和复性过程，该探针利用血红素衍生的四吡咯化合物biliverdin作为发色团。 iRFP包含一个独特的八字形结。 iRFP异形体的变性和复性曲线吻合得很好，表明有效的重折叠。但是，iRFP全息形式表现出不可逆的展开和聚集与绑定发色团相关联。无融合蛋白的结结构不能阻止biliverdin的后续结合，导致功能性iRFP呈全同形。我们建议蛋白质解折叠的不可逆性是由翻译后蛋白质修饰（例如生色团结合）引起的，而不是由结的存在引起的。这些结果对于基于BphP的近红外探针的未来设计至关重要，并为我们的蛋白质折叠知识增加了重要特征。

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