Bacillus species belong to the branch of Gram-positive bacteria known as firmicutes that are characterised by a low G+C content in their DNA. They are used as model organisms for studying bacterial cell biology and have an unusual life cycle that ends with endospore formation. Bacillus species cause important diseases including anthrax (Bacillus anthracis) and are important industrial organisms, with B. subtilis and B. megaterium in particular, used for the production of enzymes and other useful proteins. They are notable for producing large amounts of secreted proteins that can be easily purified from the growth medium (Bacillus cells have only one cell membrane). Researchers at UEA (led by Matt Hutchings) are attempting to exploit their protein production and secretion capabilities to produce large amounts of heterologous proteins. Bacillus species, particularly Bacillus subtilis, have become model organisms for studies of Gram-positive bacteria. Nick Le Brun's group at UEA has studied several fundamental aspects of the biology of Gram-positive bacteria using B. subtilis. These include: the management of disulfide bonds (making and breaking) on the outside of the cytoplasmic membrane; the maturation of c-type cytochromes, which takes place on the outside of the cytoplasmic membrane and occurs via a complex mechanism that is distinct from that of higher eukaryotes, and copper trafficking/detoxification systems that ensure that this essential but potentially highly toxic metal ion is maintained within the cell in a safe form.
PATENT GB1007379.9: Widdick D.A., Palmer T. and Hutchings M.I. (2010). Bacterial secretion.
Singleton, C., Hearnshaw, S., Zhou, L., Le Brun, N.E. and Hemmings, A.M. (2009). Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA. Biochem. J. 424:347-356
Crow, A., Lewin, A., Hecht, O., Carlsson Möller, M., Moore, G.R., Hederstedt, L. and Le Brun, N.E. (2009) Crystal structure and biophysical properties of Bacillus subtilis BdbD: An oxidizing thiol:disulfide oxidoreductase containing a novel metal site. J. Biol. Chem. 284:23719-23733
Crow, A., Liu, Y., Carlsson Möller, M., Le Brun, N.E. and Hederstedt, L. (2009) Structure and functional properties of Bacillus subtilis endospore-biogenesis factor StoA. J. Biol. Chem. 284:10056-10066.
Hodson, C.T.C., Lewin, A., Hederstedt, L. and Le Brun, N.E. (2008) The active site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilis. J. Bacteriol. 190:4697-4705.