We present the first proteome-wide characterization of protein localization dynamics. We exploit time-lapse fluorescence microscopy and automated image analysis tools to capture protein localization dynamics throughout the cell cycle in hundreds of single cells for all proteins in E. coli with non-diffuse localization. This approach distinguishes between cell-to-cell variation and cell-cycle dynamics. We compute a distance between all imaged localization patterns, which facilitates the comparison of average protein localization patterns between proteins, including both temporal and spatial structure. Globally, the analysis of these patterns reveals many significant but subtle variations in well established patterns of localization suggesting a large number of mechanisms of protein localization, the majority of which are robust to protein copy number. Finally, we analyze the protein partitioning at cell division and find that in addition to many factors which are retained preferentially in the mother (the cell with the oldest pole) a number of proteins preferentially partition to the daughter. The biological significance of these asymmetries is not yet understood. In addition to the results reported in this paper, we have built a publicly-accessible online database which provides raw and processed data to the research community.

Localizome site.

Reference: NJ Kuwada, B Traxler, and PA Wiggins. Genome-scale quantitative characterization of bacterial protein localization dynamics throughout the cell cycle. Molecular Microbiology 95(1):64-79 (2015)