Light-activated reassembly of split green fluorescent protein.
Light-activated reassembly of split green fluorescent protein.
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DOI：
10.1021/ja110256c
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发表时间：
2011-03-23
影响因子：
15
通讯作者：
Boxer SG
中科院分区：
文献类型：
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作者：
Kent KP;Boxer SG
去除第11条β链的截短绿色荧光蛋白（GFP）在生物偶联、成像以及制备具有新的光谱或功能特性的半合成蛋白质方面具有潜在的意义。令人惊讶的是，通过去除第11条链产生的截短的GFP一旦重折叠，就不会与对应于链11的合成肽重新组装，而是在光活化后重新组装。通过吸收光谱、荧光光谱和拉曼光谱对这一过程的机理进行了详细的研究。在这个重折叠的截短的绿色荧光蛋白的发色团被发现是在反式构型。在暴露于光时，在发色团的反式和顺式构象之间形成光稳态，并且仅具有发色团的顺式构型的截短的GFP结合肽。一个动力学模型描述的光激活重组的分裂GFP进行了讨论。这种独特的光驱动的重组对于控制蛋白质-蛋白质相互作用是潜在有用的。
Truncated Green Fluorescent Protein (GFP) with the 11th β-strand removed is potentially interesting for bioconjugation, imaging, and the preparation of semi-synthetic proteins with novel spectroscopic or functional properties. Surprisingly, the truncated GFP generated by removing the 11th strand, once refolded, does not reassemble with a synthetic peptide corresponding to strand 11, but does reassemble following light activation. The mechanism of this process has been studied in detail by absorption, fluorescence and Raman spectroscopy. The chromophore in this refolded truncated GFP is found to be in the trans configuration. Upon exposure to light a photostationary state is formed between the trans and cis conformations of the chromophore, and only truncated GFP with the cis configuration of the chromophore binds the peptide. A kinetic model describing the light activated reassembly of this split GFP is discussed. This unique light-driven reassembly is potentially useful for controlling protein-protein interactions.
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