Supporting data for Organotellurium Probes Enable One-step Single-cell Analysis of Post-translational Modification

Protein prenylation is a widespread post-translational modification that regulates membrane association and signal-ing; dysregulation of this process leads to a variety of diseases. Metabolic labeling with probes containing bioorthog-onal functionality has revolutionized the study of many protein modifications including prenylation. However, that approach requires two steps including metabolic incorporation and subsequent bioorthogonal reaction to install chemical reporters. Here, the development and use of a suite of tellurium-containing analogues that can be incorpo-rated into proteins in a single step and employed to directly measure global prenylation levels in cells via mass cy-tometry is described. This robust methodology was examined in a variety of cell lines and used to show that prenyla-tion levels are perturbed in autophagy-deficient L6 cells, a model for aging. Modification of tellurium-labeled pro-teins through the oxidation-controlled, strain-promoted tellurophene-alkyne cycloaddition reaction also enabled identification of prenylation targets by chemical proteomics. This dataset contains all raw and processed data supporting the findings of the manuscript. It includes CyTOF mass cytometry files from multiple cell lines (WT and Atg7 KO L6, AML-3, MOLM-13, AML-12, and COS-7), gel fluorescence images, fluorescence-based enzymatic assay and steady-state kinetic measurements, as well as NMR and HRMS data for all synthesized compounds. Data package also includes western blot analyses and molecular docking results. Together, these datasets provide comprehensive experimental evidence for the synthesis, characterization, and functional evaluation of tellurium-based chemical probes used in this study.