Characterization of acyl carrier protein expression during sporulation in Bacillus subtilis

MARIANO MARTINEZ,; SCHUJMAN, GE; DE MENDOZA, D

Pinamar

Congreso; X Congress of Panamerican Association for Biochemistry and Molecular Biology (PABMB) – 41th annual meeting of SAIB; 2005

The acyl carrier protein (ACP) plays a key role in fatty acids biosynthesis, linking all the intermediates and presenting them to different enzymes of this metabolic pathway. We have shown that sporulation, a differentiation process in Bacillus subtilis, requires de novo fatty acids biosynthesis, and by fluorescence microscopy we found that ACP is synthesized only in the mother cell compartment. In order to understand this observation, we constructed a transcriptional fusion of the acp promoter to GFP and we found that its compartmentalization is due to a preferential transcription of the gene in the mother cell. The same expression pattern was observed in mutants of sigE (mother cell specific) and sigF (preespore specific) transcriptions factor, indicating that other mechanism regulate acp expression. By gel shift assays we determined the existence of a sporulation specific protein able to bind to the acp promoter, and that we purified and identified. These results suggest that there is a regulatory mechanism that govern ACP expression during sporulation in B. subtilis.