Trigger Factor from Thermus thermophilus Is a Zn2+-dependent Chaperone*
Trigger Factor from Thermus thermophilus Is a Zn2+-dependent Chaperone*
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嗜热栖热菌的触发因子是 Zn2 依赖性伴侣*
DOI：
10.1074/jbc.m311572200
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发表时间：
2004
影响因子：
4.8
通讯作者：
Masasuke Yoshida
中科院分区：
文献类型：
--
作者：
Ryoji Suno;H. Taguchi;R. Masui;M. Odaka;Masasuke Yoshida
大肠杆菌的核糖体相关伴侣触发因子（TF）与各种新合成的多肽相互作用，以帮助其正确折叠。在这里，我们报告的TF的嗜热真细菌，嗜热栖热菌，逮捕自发折叠的绿色荧光蛋白形成1：1的二元复合物。该复合物可通过凝胶过滤分离，但由于α-酪蛋白大量释放绿色荧光蛋白，因此显示为动态的。出乎意料的是，EDTA完全消除了TF的折叠停滞活性，分析表明，我们制备的TF含有约0.5 mol Zn ~（2+）/mol TF。用Zn ~（2+）饱和的TF（~ 1 mol/mol TF）的折叠阻滞活性是未处理的TF的两倍。因此，嗜热TF的分子伴侣活性是Zn 2+依赖性的。
The ribosome-associated chaperone trigger factor (TF) of Escherichia coli interacts with a variety of newly synthesized polypeptides to assist their correct folding. Here, we report that the TF of thermophilic eubacterium, Thermus thermophilus, arrested spontaneous folding of green fluorescent protein by forming a 1:1 binary complex. The complex was isolable by gel-filtration but was shown to be dynamic because green fluorescent protein was released by α-casein in large excess. Unexpectedly, EDTA completely abolished the folding-arrest activity of TF, and analysis revealed that the TF from our preparation contained ∼0.5 mol Zn2+/mol TF. The folding-arrest activity of TF that was saturated with Zn2+ (∼1 mol/mol TF) was twice as efficient as that of untreated TF. Thus, chaperone activity of thermophilic TF is Zn2+-dependent.
牛心 F1-ATP 酶上的腺嘌呤核苷酸结合位点。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Cross,RL;Nalin,CM
通讯作者：
Nalin,CM