Genetic links between bacterial dynamin and flotillin proteins.

Dynamin is a membrane-associated GTPase that confers motor-like functions in membrane dynamics, such as endocytosis, in eukaryotic cells. Flotillin (reggie) proteins are also a widely conserved class of membrane proteins, associated with the formation of protein assemblies within the membrane, and with endocytotic processes. Bacterial dynamin has been shown to bind to membranes in vitro and to mediate membrane fusion. Bacillus subtilis DynA localizes to the cell division septum, and it was recently shown that it indeed plays a role in cell division. Interestingly, dynamin shows a genetic interaction with flotillin proteins in this prokaryotic model organism and the absence of both proteins results in a cell division and cell shape defect. Here, we show that in addition to the morphological phenotypes, a dynamin/flotillin double deletion strain shows a synthetic defect in cell motility, much stronger than that of flotillin single mutant cells. While the contribution of altered cell shape and slower growth of the double deletion strain on motility cannot be clearly assessed, our data emphasize the fact that dynamin and flotillin proteins play tightly connected functions in a wide range of aspects in membrane processes in bacteria.