JOURNAL ARTICLE

The extracellular proteome of Bacillus licheniformis grown in different media and under different nutrient starvation conditions

Birgit Voigt, Thomas Schweder, Mark J J B Sibbald, Dirk Albrecht, Armin Ehrenreich, Jörg Bernhardt, Jörg Feesche, Karl-Heinz Maurer, Gerhard Gottschalk, Jan Maarten van Dijl, Michael Hecker
Proteomics 2006, 6 (1): 268-81
16317772
The now finished genome sequence of Bacillus licheniformis DSM 13 allows the prediction of the genes involved in protein secretion into the extracellular environment as well as the prediction of the proteins which are translocated. From the sequence 296 proteins were predicted to contain an N-terminal signal peptide directing most of them to the Sec system, the main transport system in Gram-positive bacteria. Using 2-DE the extracellular proteome of B. licheniformis grown in different media was studied. From the approximately 200 spots visible on the gels, 89 were identified that either contain an N-terminal signal sequence or are known to be secreted by other mechanisms than the Sec pathway. The extracellular proteome of B. licheniformis includes proteins from different functional classes, like enzymes for the degradation of various macromolecules, proteins involved in cell wall turnover, flagellum- and phage-related proteins and some proteins of yet unknown function. Protein secretion is highest during stationary growth phase. Furthermore, cells grown in complex medium secrete considerably higher protein amounts than cells grown in minimal medium. Limitation of phosphate, carbon and nitrogen sources results in the secretion of specific proteins that may be involved in counteracting the starvation.

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