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• W2016880029 abstract "Nucleotide-binding proteins play pivotal roles in many cellular processes including cell signaling. However, targeted studies of the subproteome of nucleotide-binding proteins, especially protein kinases and GTP-binding proteins, remain challenging. Here, we report a general strategy in using affinity-labeled chemical probes to enrich, identify, and quantify ATP- and GTP-binding proteins in the entire human proteome. Our results revealed that the ATP/GTP affinity probes facilitated the identification of 100 GTP-binding proteins and 206 kinases with the use of low milligram quantities of lysate of HL-60 cells. In combination with the use of the stable isotope labeling by amino acids in cell culture-based quantitative proteomics method, we assessed the ATP/GTP binding selectivities of nucleotide-binding proteins at the global proteome scale. Our results confirmed known and, more importantly, unveiled new ATP/GTP-binding preferences of hundreds of nucleotide-binding proteins. Additionally, our strategy led to the identification of three and one unique nucleotide-binding motifs for kinases and GTP-binding proteins, respectively, and the characterizations of the nucleotide-binding selectivities of individual motifs. Our strategy for capturing and characterizing ATP/GTP-binding proteins should be generally applicable for those proteins that can interact with other nucleotides." @default.
• W2016880029 created "2016-06-24" @default.
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• W2016880029 date "2013-02-28" @default.
• W2016880029 modified "2023-10-14" @default.
• W2016880029 title "Proteome-Wide Discovery and Characterizations of Nucleotide-Binding Proteins with Affinity-Labeled Chemical Probes" @default.
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• W2016880029 doi "https://doi.org/10.1021/ac303383c" @default.
• W2016880029 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3606491" @default.
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