Cysteine 397 plays important roles in the folding of the neuron-restricted silencer factor/RE1-silencing transcription factor.
Cysteine 397 plays important roles in the folding of the neuron-restricted silencer factor/RE1-silencing transcription factor.
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半胱氨酸 397 在神经元限制性沉默因子/RE1 沉默转录因子的折叠中发挥重要作用。
DOI：
10.1016/j.bbrc.2011.09.045
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发表时间：
2011
影响因子：
3.1
通讯作者：
C. Cao
中科院分区：
文献类型：
--
作者：
Yan Zhang;Wei Hu;Jie Shen;X. Tong;Zhongzheng Yang;Z. Shen;W. Lan;Houming Wu;C. Cao
神经元限制性沉默因子/RE1沉默转录因子（NRSF/REST）不仅被认为是一个关键的转录抑制因子，而且通过特异性地与神经元限制性沉默元件（NRSE/RE1） dsDNA和小NRSE/RE1 dsRNA相互作用，成为神经元基因表达的激活因子。但其确切机制尚不清楚。一个主要的问题是很难获得其功能的多锌指结构域，以供进一步的结构研究。为了解决这一问题，在本研究中，我们首次通过圆二色（CD）光谱和二维（2D）核磁共振（NMR） 1H-1H noesi光谱监测每个ZnF肽的折叠，分别获得了含有4、5、6和7个ZnF基序的可溶性NRSF/REST功能域，分别为ZnF5-8、ZnF4-8、ZnF3-8和ZnF2-8。这些数据表明，残基半胱氨酸397 （Cys397）在NRSF/REST多个ZnFs结构域的全局折叠中起重要作用。
The neuron-restrictive silencer factor/RE1-silencing transcription factor (NRSF/REST) is regarded as not only a key transcriptional repressor but also an activator in neuron gene expression by specifically interacting with neuron-restrictive silencer element (NRSE/RE1) dsDNA and small NRSE/RE1 dsRNA, respectively. But its exact mechanism remains unclear. One major problem is that it is hard to obtain its functional multiple zinc finger (ZnF) domains in a large quantity for further structural studies. To address this issue, in this study, we for the first time attained soluble NRSF/REST functional domains named as ZnF5–8, ZnF4–8, ZnF3–8 and ZnF2–8 containing four, five, six and seven ZnF motifs in tandem, respectively, by using Circular Dichroism (CD) spectrum and two-dimensional (2D) nucleic magnetic resonance (NMR)1H–1H NOESY spectrum to monitor the folding of each single ZnF peptide. The data indicated that the residue cysteine 397 (Cys397) plays important roles in the global folding of NRSF/REST multiple ZnFs domain.