Disease relevance of Bacillin

• We found that a polycistronic operon (ywfBCDEFG) and a monocistronic gene (ywfH) are required for the biosynthesis of bacilysin in Bacillus subtilis [1].
• We propose that, unlike antibiotic production in Streptomyces spp., bacilysin production in B. subtilis is controlled by a dual regulation system composed of the guanine nucleotides ppGpp and GTP [1].
• The data indicate that tetaine enters E. coli cells predominantly by dipeptide permease and in part by one or more oligopeptide permease system [2].
• Transport and metabolism of bacilysin and other peptides by suspensions of Staphylococcus aureus [3].

High impact information on Bacillin

• In wild-type (rel(+)) cells, a forced reduction of intracellular GTP, brought about by addition of decoyinine, which is a GMP synthetase inhibitor, enhanced the expression of both the ywfBCDEFG operon and the ywfH gene, resulting in a 2.5-fold increase in bacilysin production [1].
• Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-operatively regulate the production of an antibiotic bacilysin in Bacillus subtilis [1].
• The disruption of these genes by plasmid integration caused loss of the ability to produce bacilysin, accompanied by a lack of bacilysin synthetase activity in the crude extract [1].
• Synthesis of bacilysin by Bacillus subtilis branches from prephenate of the aromatic amino acid pathway [4].
• Amplification of the bacABCDE gene cluster in a bacAB gene-deficient host strain of B. amyloliquefaciens resulted in a tenfold bacilysin overproduction [5].

Chemical compound and disease context of Bacillin

• In media with carbon source other than glucose tetaine induced of enhanced glucosamine incorporation into the cell-envelope of Escherichia coli K-12 [6].
• L-Alanyl-L-tyrosine and glycyl-L-phenylalanine labelled with 14C competed with each other and with the dipeptide antibiotic bacilysin for transport into Staphylococcus aureus NCTC 6571 in a medium which did not support growth [3].
• The antibiotic tetaine (bacilysin) and its C-terminal epoxyaminoacid--anticapsin--are powerful inhibitors of glucosamine-6-phosphate synthetase (EC 5.3.1.19.) in cell-free extracts of Escherichia coli K-12 [7].

Biological context of Bacillin

• The abrB mutation suppressed the bacilysin-negative phenotype of a spo0A mutant, whereas the same mutation in the wild-type strain resulted in a significant increase in the production of bacilysin [8].
• It is suggested that the antibacterial activity of bacilysin depends on its transport into the organism, its hydrolysis to anticapsin and on inhibition by the latter of glucosamine synthetase, and that bacilysin-resistant mutants are defective in a transport system [9].

Anatomical context of Bacillin

• The antibiotic tetaine inhibits in Candida albicans the biosynthesis of two important cell wall constituents, chitin and mannoprotein [10].
• The behaviour of these dipeptides paralleled the inactivation of bacilysin by suspensions of S. aureus and the appearance of its C-terminal amino acid, anticapsin, in the extracellular fluid [3].
• Tetaine is also an inhibitor of DNA and RNA polymerase reactions in a cell-free system, as determined using partially purified extracts from HeLa S3 cells that served as a source of the enzymes [11].

Gene context of Bacillin

• Mutant strains G21 and G23, showed a qualitatively normal, though delayed, dimorphic transition and partial cross-resistance to bacilysin [12].

Analytical, diagnostic and therapeutic context of Bacillin

• The genes bacD and bacE proved to encode the functions of amino acid ligation and self-protection to bacilysin, respectively [5].
• In a minimal medium the minimum inhibitory concentration for bacilysin with E. coli B is 10(-3) mug ml(-1) [13].

References