Citation: Mengting Pan, Yunming Liu, Xiaofang Zheng, Meijuan Zhou, Changjun You, Xiaoxia Dai. Comprehensive profiling of CTP-binding proteins using a biotinylated CTP affinity probe[J]. Chinese Chemical Letters, ;2021, 32(11): 3479-3482. doi: 10.1016/j.cclet.2021.05.057 shu

Comprehensive profiling of CTP-binding proteins using a biotinylated CTP affinity probe

State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Molecular Science and Biomedicine Laboratory, Hunan Provincial Key Laboratory of Biomacromolecular Chemical Biology, Hunan University, Changsha 410082, China

changjun@hnu.edu.cn

xiaoxiad@hnu.edu.cn

Received Date: 9 March 2021
Revised Date: 21 April 2021
Accepted Date: 24 May 2021
Available Online: 28 May 2021

Figures(4)

Recent studies have shown that CTP may act as a ligand to regulate the activity of its target proteins in many biological processes. However, proteome-wide identification of CTP-binding proteins remains challenging. Here, we employed a biotinylated CTP affinity probe coupled with stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics approach to capture, identify and quantify CTP-binding proteins in human cells. By performing two types of competitive SILAC experiments with high vs. low concentrations of CTP probe (100 vs. 10 µmol/L) or with CTP probe in the presence of free CTP, we identified 90 potential CTP-binding proteins which are involved in a variety of biological processes, including protein folding, nucleotide binding and cell-cell adhesion. Together, we developed a chemical proteomic method for uncovering the CTP-binding proteins in human cells, which could be widely applicable for profiling CTP-binding proteins in other biological samples.
- CTP-binding proteins,
- CTP affinity probe,
- Mass spectrometry,
- SILAC,
- Quantitative proteomics
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