Citation: Wang Simeng, Zhang Yanan, Zhang Longhua, Zhang Min, Tian Changlin. Conformational change of E. coli sulfurtransferase YgaP upon SCN^- in intact native membrane revealed by fluorescence lifetime and anisotropy[J]. Chinese Chemical Letters, ;2018, 29(10): 1513-1516. doi: 10.1016/j.cclet.2018.08.002 shu

Conformational change of E. coli sulfurtransferase YgaP upon SCN^- in intact native membrane revealed by fluorescence lifetime and anisotropy

Wang Simeng ^a ,
Zhang Yanan ^b ,
Zhang Longhua ^b ,
Zhang Min ^a,, ,
Tian Changlin ^b,c,*,,

a.
School of Life Science, Anhui University, Hefei 230039, China
b.
National Laboratory of Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei 230027, China
c.
High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China

Corresponding author: Zhang Min, zhmin07@ahu.edu.cn Tian Changlin, cltian@ustc.edu.cn

Received Date: 4 June 2018
Revised Date: 1 August 2018
Accepted Date: 2 August 2018
Available Online: 3 October 2018

Figures(4)

Fluorescence lifetime and anisotropy has become a prevalent tool to detect the structure change and motility property of proteins. YgaP is the only membrane-integrated rhodanese in E. coli. The sulfur transfer process has been characterized by various studies. However, the mechanism of the outward transportation of SCN^- remains unclear. In this work, we examined the fluorescence lifetime and anisotropy of site-specific incorporated unnatural amino acid 7-HC to study the conformational change of YgaP upon SCN^- binding. We also compared the fluorescence changes between detergent-wrapped environment in DPC and intact native membrane environment in SMA. Our results suggested the presence of at least two different conformations in YgaP protein. Both the residues in the middle of TMH2 and the residues near extracellular side play important roles in the binding and/or output of SCN^-. SMA is a good material to reflect the in situ conformation changes of protein than micelles.
- Rhodanese YgaP,
- Fluorescence lifetime and anisotropy,
- SMA,
- Conformation change
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通讯作者: 陈斌, bchen63@163.com

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沈阳化工大学材料科学与工程学院沈阳 110142

Conformational change of E. coli sulfurtransferase YgaP upon SCN- in intact native membrane revealed by fluorescence lifetime and anisotropy

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通讯作者: 陈斌, bchen63@163.com

Conformational change of E. coli sulfurtransferase YgaP upon SCN^- in intact native membrane revealed by fluorescence lifetime and anisotropy