Abstract
SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.
Highlights
In response to starvation conditions, Bacillus subtilis cells cease vegetative growth and initiate the formation of a dormant cell type called a spore [1,2,3]
In this short paper we investigate the role of a metal cofactor in both functions of SpoIIE
We purified the entire cytoplasmic part of the SpoIIE protein, which consists of two domains that are involved in oligomerization and interaction with FtsZ [21] and in dephosphorylation of SpoIIAA-P [19]
Summary
In response to starvation conditions, Bacillus subtilis cells cease vegetative growth and initiate the formation of a dormant cell type called a spore [1,2,3]. Compartment specific transcription factors σF and σE are activated in the forespore and in the mother cell, respectively. This activation event is critical because it initiates the rest of the sporulation developmental program in each daughter cell. The cell division protein FtsZ, that during vegetative growth drives the mid-cell division, switches its position to the polar sites of the cell. At the onset of sporulation, SpoIIE co-localizes with FtsZ at mid-cell and both proteins redeploy to polar sites via a spiral-like intermediate [4]. It was shown that this process requires DivIVA, which interacts
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