Far from being well-mixed, almost all biological systems exhibit precise spatial and temporal control of protein, mRNA, and DNA concentration, demonstrating that cells measure distance and detect proximity with a molecular-scale tool kit. Despite its relatively simple cellular structure and small size, Escherichia coli exhibits a high degree of spatial organization. When cellular ultra-structure is disrupted, there are profound functional consequences, from abnormal gene expression to the failure to efficiently segregate the chromosome on the completion of replication.
In this talk I will describe work my lab has performed capturing the dynamic localization of nearly all E. coli proteins with non-diffuse localization. This protein atlas reveals a surprisingly complex repertoire of dynamic protein localization. In addition to the discovery of novel protein localization patterns, we have found uncharacterized proteins co-localized with proteins of known function. Our data also provides insight into the temporal ordering of assembly of protein ultra-structure as well as characterizing the partitioning of proteins at cell division for the first time on a proteome-wide scale. Finally, I will discuss applications of our technology to screening and gene discovery.