DivIVA Regulates Its Expression and the Orientation of New Septum Growth in Deinococcus radiodurans.

In rod-shaped Gram-negative bacteria, FtsZ localization at midcell position is regulated by the gradient of MinCDE complex across the poles. In round-shaped bacteria, which lack predefined poles, the next plane of cell division is perpendicular to the previous plane, and determination of the FtsZ assembly site is still intriguing. Deinococcus radiodurans, a coccus bacterium, is characterized by its extraordinary resistance to DNA damage. DivIVA, a putative component of the Min system in this bacterium, interacts with cognate cell division and genome segregation proteins. Here, we report that deletion of a chromosomal copy of DivIVA was possible only when the wild-type copy of DivIVA was expressed in on a plasmid. However, deletion of the C-terminal domain (CTD) of DivIVA (CTD mutant) was possible but produced distinguishable phenotypes, like smaller cells, slower growth, and tilted septum orientation, in D. radiodurans. In expression of DivIVA in the CTD mutant could restore these features of the wild type. Interestingly, the overexpression of DivIVA led to delayed separation of tetrads from an octet state in both -complemented -mutant and wild-type cells. The CTD mutant showed upregulation of the operon. Both the wild type and CTD mutant formed FtsZ foci; however, unlike wild type, the position of foci in the mutant cells was found to be away from conjectural midcell position in cocci. Notably, DivIVA-red fluorescent protein (DivIVA-RFP) localizes to the septum during cell division at the new division site. These results suggested that DivIVA is an essential protein in D. radiodurans, and its C-terminal domain plays an important role in the regulation of its expression and orientation of new septal growth in this bacterium. In rod-shaped Gram-negative bacteria, the midcell position for binary fission is relatively easy to model. In cocci that do not have predefined poles, the plane of next cell division is shown to be perpendicular to the previous plane. However, the molecular basis of perpendicularity is not known in cocci. The DivIVA protein of Deinococcus radiodurans, a coccus bacterium, physically interacts with the septum and establishes macromolecular interactions with genome segregation proteins through its N-terminal domain and with MinC through the C-terminal domain. Here, we have brought forth some evidence to suggest that DivIVA is essential for growth and plays an important role in cell polarity determination, and its C-terminal domain plays a crucial role in the growth of new septa in the correct orientation as well as in the regulation of DivIVA expression.