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Background  The Gram-positive facultative methylotrophic bacterium  Bacillus methanolicus  uses the sedoheptulose-1,7-bisphosphatase (SBPase) variant of the ribulose monophosphate (RuMP) cycle for growth on the C 1  carbon source methanol. Previous genome sequencing of the physiologically different  B. methanolicus  wild-type strains MGA3 and PB1 has unraveled all putative RuMP cycle genes and later, several of the RuMP cycle enzymes of MGA3 have been biochemically characterized. In this study, the focus was on the characterization of the transaldolase (Ta) and its possible role in the RuMP cycle in  B. methanolicus .    Results  The Ta genes of  B. methanolicus  MGA3 and PB1 were recombinantly expressed in  Escherichia coli , and the gene products were purified and characterized. The PB1 Ta protein was found to be active as a homodimer with a molecular weight of 54 kDa and displayed K M  of 0.74 mM and V max  of 16.3 U/mg using Fructose-6 phosphate as the substrate. In contrast, the MGA3 Ta gene, which encodes a truncated Ta protein lacking 80 amino acids at the N-terminus, showed no Ta activity. Seven different mutant genes expressing various full-length MGA3 Ta proteins were constructed and all gene products displayed Ta activities. Moreover, MGA3 cells displayed Ta activities similar as PB1 cells in crude extracts.    Conclusions  While it is well established that  B. methanolicus  can use the SBPase variant of the RuMP cycle this study indicates that  B. methanolicus  possesses Ta activity and may also operate the Ta variant of the RuMP.

Transaldolase in Bacillus methanolicus: biochemical characterization and biological role in ribulose monophosphate cycle