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Updated: Aug 18, 2026

The MultiBac Protein Complex Production Platform at the EMBL
Published on: July 11, 2013
The Bacillus subtilis regulator protein SpoIIE shares functional and structural similarities with eukaryotic protein
R Schroeter1, S Schlisio, I Lucet
1Institut für Biologie, Humboldt Universität Berlin, Germany.
Abstract:
Dephosphorylation of SpoIIAA-P by SpoIIE is strictly dependent on the presence of the bivalent metal ions Mn2+ or Mg2+. Replacement by Ala of one of the four Asp residues, invariant in all representatives of protein phosphatase 2C, completely abolished the SpoIIE phosphatase activity in vitro, whilst replacement of the Asp residues by another acidic amino acid, Glu, had varying effects on the activities of the resulting mutated proteins. D610E and D795E exhibited some residual activity while D628E and D745E were without enzymatic activity. The results suggest that the functional model in which metal-associated water molecules are involved in the dephosphorylation reaction catalyzed by human protein phosphatase 2C alpha can also be applied to the bacterial protein phosphatase 2C-like protein.
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