Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel
Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel
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DOI：
10.1038/srep01989
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发表时间：
2013-06-17
影响因子：
4.6
通讯作者：
Mahalakshmi, Radhakrishnan
中科院分区：
文献类型：
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作者：
Maurya, Svetlana Rajkumar;Chaturvedi, Deepti;Mahalakshmi, Radhakrishnan
脂蛋白相互作用对膜蛋白的折叠、稳定性和功能至关重要，它可以是机械和化学性质的。脂质系统的力学性能可以适当地受到物理因素的影响，从而促进膜蛋白的折叠。我们在这里证明，通过加热瞬时调节脂质动力学，两种8链跨膜β -桶蛋白OmpX和OmpA（1-171）在胶束和囊泡中的快速折叠可以在几秒钟内实现。使用这种“热冲击”方法的折叠动力学显示，再折叠率增加了10到数百倍，折叠效率接近100%。我们确定，这样折叠的OmpX即使在洗涤剂胶束中也具有高度的热稳定性，并保留了与双层蛋白质相当的结构特征。
Lipid-protein interactions, critical for the folding, stability and function of membrane proteins, can be both of mechanical and chemical nature. Mechanical properties of lipid systems can be suitably influenced by physical factors so as to facilitate membrane protein folding. We demonstrate here that by modulating lipid dynamics transiently using heat, rapid folding of two 8-stranded transmembrane beta-barrel proteins OmpX and OmpA(1-171), in micelles and vesicles, can be achieved within seconds. Folding kinetics using this 'heat shock' method shows a dramatic ten to several hundred folds increase in refolding rate along with similar to 100% folding efficiency. We establish that OmpX thus folded is highly thermostable even in detergent micelles, and retains structural characteristics comparable to the protein in bilayers.