CutA1蛋白具有超热稳定性，其变性温度接近150摄氏度。
Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C.
作者信息
Tanaka Tomoyuki, Sawano Masahide, Ogasahara Kyoko, Sakaguchi Yasushi, Bagautdinov Bagautdin, Katoh Etsuko, Kuroishi Chizu, Shinkai Akeo, Yokoyama Shigeyuki, Yutani Katsuhide
机构信息
RIKEN SPring-8 Center, Harima Institute, Kouto, Sayo, Hyogo 679-5148, Japan.
出版信息
FEBS Lett. 2006 Jul 24;580(17):4224-30. doi: 10.1016/j.febslet.2006.06.084. Epub 2006 Jul 5.
We found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high denaturation temperature (T(d)) of nearly 150 degrees C, which exceeds the highest record determined by DSC by about 30 degrees C. To elucidate the mechanism of the ultra-high stability of PhCutA1, we analyzed the crystal structures of CutA1 proteins from three different sources, P. horikoshii, Thermus thermophilus, and Escherichia coli, with different growth temperatures (98, 75, and 37 degrees C). This analysis revealed that the remarkably increased number of ion pairs in the monomeric structure contributes to the stabilization of the trimeric structure and plays an important role in enhancing the T(d), up to 150 degrees C, for PhCutA1.
我们发现，来自嗜热栖热菌的CutA1蛋白（PhCutA1）具有近150℃的极高变性温度（T(d)），这比差示扫描量热法（DSC）测定的最高记录高出约30℃。为阐明PhCutA1超高稳定性的机制，我们分析了来自三种不同来源（生长温度分别为98℃、75℃和37℃）的嗜热栖热菌、嗜热栖热放线菌和大肠杆菌的CutA1蛋白的晶体结构。该分析表明，单体结构中显著增加的离子对数量有助于三聚体结构的稳定，并在将PhCutA1的T(d)提高到150℃方面发挥重要作用。
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