Toggle Main Menu Toggle Search

Open Access padlockePrints

The cell differentiation protein SpoIIE contains a regulatory site that controls its phosphatase activity in response to asymmetric septation

Lookup NU author(s): Professor Jeff Errington FRSORCiD


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Starvation induces Bacillus subtilis to initiate a -simple, two-cell developmental process that begins with an asymmetric cell division. Activation of the first compartment-specific transcription factor, sigmaF, is coupled to this morphological event. SpoIIE, a bifunctional protein, is essential for the compartment-specific activation of sigmaF and also has a morphogenic activity required for asymmetric cell division. SpoIIE consists of three domains: a hydrophobic N-terminal domain, which targets the protein to the membrane; a central domain, involved in oligomerization of SpoIIE and interaction with the cell division protein FtsZ; and a C-terminal domain comprising a PP2C protein phosphatase. Here, we report the isolation of mutations at the very beginning of the central domain of spoIIE, which are capable of activating sigmaF inde-pendently of septum formation. Purified mutant proteins showed the same phosphatase activity as the wild-type protein in vitro. The mutant proteins were fully functional in respect of their localization to sites of asymmetric septation and support of asymmetric division. The data provide strong evidence that the phosphatase domain of SpoIIE is tightly regulated in a way that makes it respond to the formation of the asymmetric septum.

Publication metadata

Author(s): Feucht A, Abbotts L, Errington J

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2002

Volume: 45

Issue: 4

Pages: 1119-1130

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Wiley-Blackwell Publishing Ltd.


DOI: 10.1046/j.1365-2958.2002.03082.x


Altmetrics provided by Altmetric