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Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis
The crystal structure of the phosphatase domain of SpoIIE is determined, revealing a domain-swapped dimer and a clustering of sites whose point mutation interferes with the proper coupling of asymmetric septum formation to sigma factor activation and identifies a surface involved in intramolecular signaling.
Expression of soluble, active fragments of the morphogenetic protein SpoIIE from Bacillus subtilis using a library-based construct screen
Over 9000 genetic constructs of spoIIE are screened using a random incremental truncation library approach, ESPRIT, to identify a number of soluble C-terminal fragments of SpoIIE that were aligned with the protein sequence to map putative domains and domain boundaries.
Structure and activity investigations of the cell fate determinant, SpoIIE, from Bacillus subtilis
The isolation and characterisation of three new fragments of spoIIE containing elements of the central cytoplasmic domain of SpoIIE are described, including a fragment found to accurately represent the N-terminal solubility limit of domain II which shows a high degree of oligomeric character.