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Mol Microbiol


Title:"Bacillus subtilis antibiotics: structures, syntheses and specific functions"
Author(s):Stein T;
Address:"Institut fur Mikrobiologie, Johann Wolfgang Goethe-Universitat, Marie-Curie-Strasse 9, 60439 Frankfurt/Main, Germany. T.Stein@em.uni-frankfurt.de"
Journal Title:Mol Microbiol
Year:2005
Volume:56
Issue:4
Page Number:845 - 857
DOI: 10.1111/j.1365-2958.2005.04587.x
ISSN/ISBN:0950-382X (Print) 0950-382X (Linking)
Abstract:"The endospore-forming rhizobacterium Bacillus subtilis- the model system for Gram-positive organisms, is able to produce more than two dozen antibiotics with an amazing variety of structures. The produced anti-microbial active compounds include predominantly peptides that are either ribosomally synthesized and post-translationally modified (lantibiotics and lantibiotic-like peptides) or non-ribosomally generated, as well as a couple of non-peptidic compounds such as polyketides, an aminosugar, and a phospholipid. Here I summarize the structures of all known B. subtilis antibiotics, their biochemistry and genetic analysis of their biosyntheses. An updated summary of well-studied antibiotic regulation pathways is given. Furthermore, current findings are resumed that show roles for distinct B. subtilis antibiotics beyond the 'pure' anti-microbial action: Non-ribosomally produced lipopeptides are involved in biofilm and swarming development, lantibiotics function as pheromones in quorum-sensing, and a 'killing factor' effectuates programmed cell death in sister cells. A discussion of how these antibiotics may contribute to the survival of B. subtilis in its natural environment is given"
Keywords:Amino Acid Sequence *Anti-Bacterial Agents/chemistry/metabolism Bacillus subtilis/genetics/*metabolism *Bacterial Proteins/chemistry/genetics/metabolism Bacteriocins/chemistry/genetics/metabolism Humans Molecular Sequence Data Molecular Structure *Peptide;
Notes:"MedlineStein, Torsten eng Review England 2005/04/28 Mol Microbiol. 2005 May; 56(4):845-57. doi: 10.1111/j.1365-2958.2005.04587.x"

 
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