【摘 要】
：
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 affini
【机 构】
：
State Key Laboratory of Chemo/Biosensing and Chemometrics,College of Chemistry and Chemical Engineer
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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.
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