scholarly journals Biochemical and Genetic Characterization of an Auxotroph of Bacillus subtilis Altered in the Acyl-CoA:Acyl-Carrier-Protein Transacylase

2005 ◽  
Vol 115 (1) ◽  
pp. 175-182 ◽  
Author(s):  
Don P. BOUDREAUX ◽  
Ernst FREESE ◽  
Eric EISENSTADT ◽  
Tadako IIJIMA
1999 ◽  
Vol 65 (9) ◽  
pp. 4288-4291 ◽  
Author(s):  
David H. Green ◽  
Phil R. Wakeley ◽  
Anthony Page ◽  
Andrew Barnes ◽  
Loredana Baccigalupi ◽  
...  

ABSTRACT Bacillus subtilis is currently used as an oral probiotic. We examined two commercial B. subtilis probiotic preparations, Enterogermina and Biosubtyl. Surprisingly, physiological and genetic characterization of the bacteria contained in each of these preparations has shown that neither contains B. subtilis.


Microbiology ◽  
1997 ◽  
Vol 143 (10) ◽  
pp. 3231-3240 ◽  
Author(s):  
J. Muller ◽  
S. Schiel ◽  
G. W. Ordal ◽  
H. H. Saxild

Microbiology ◽  
2010 ◽  
Vol 156 (2) ◽  
pp. 484-495 ◽  
Author(s):  
Mariano A. Martinez ◽  
Diego de Mendoza ◽  
Gustavo E. Schujman

Acyl carrier protein (ACP) is a universal and highly conserved carrier of acyl intermediates during fatty acid biosynthesis. The molecular mechanisms of regulation of the acpP structural gene, as well as the function of its gene product, are poorly characterized in Bacillus subtilis and other Gram-positive organisms. Here, we report that transcription of acpP takes place from two different promoters: PfapR and PacpP. Expression of acpP from PfapR is coordinated with a cluster of genes involved in lipid synthesis (the fapR operon); the operon consists of fapR-plsX-fabD-fabG-acpP. PacpP is located immediately upstream of the acpP coding sequence, and is necessary and sufficient for normal fatty acid synthesis. We also report that acpP is essential for growth and differentiation, and that ACP localizes in the mother-cell compartment of the sporangium during spore formation. These results provide the first detailed characterization of the expression of the ACP-encoding gene in a Gram-positive bacterium, and highlight the importance of this protein in B. subtilis physiology.


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