
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. Even bacterial cells, with neither sub-cellular organelles nor cytoskeletal motors, exert concerted and often precise control over both spatial and temporal sub-cellular 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 first describe a number of known physical mechanisms of cellular organization in bacterial cells and how the chemistry of nanometer-scale interactions between proteins encodes micron-scale cellular structure. In the second half of 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.

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. Even bacterial cells, with neither sub-cellular organelles nor cytoskeletal motors, exert concerted and often precise control over both spatial and temporal sub-cellular 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 first describe a number of known physical mechanisms of cellular organization in bacterial cells and how the chemistry of nanometer-scale interactions between proteins encodes micron-scale cellular structure. In the second half of 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.