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The cell differentiation protein SpoIIE contains a regulatory site that controls its phosphatase activity in response to asymmetric septation
Author(s) -
Feucht Andrea,
Abbotts Laura,
Errington Jeffery
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.03082.x
Subject(s) - biology , microbiology and biotechnology , phosphatase , cell division , transcription factor , mutant , bacillus subtilis , ftsz , cell , biochemistry , genetics , gene , phosphorylation , bacteria
Summary 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, σ F , is coupled to this morphological event. SpoIIE, a bifunctional protein, is essential for the compartment‐specific activation of σ F 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 σ F independently 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.