Functions of the peptide antibiotics tyrocidine and gramicidin. Induction of conformational and structural changes of superhelical DNA.

The peptide antibiotic tyrocidine which is produced by Bacillus brevis and is probably involved in sporogenesis, unwinds superhelical plasmids in vitro at low peptide: DNA ratios, as found by gel electrophoresis. At higher peptide concentrations, the DNA is packed tightly leading to apparent nuclease stability of the complex and inhibition of RNA synthesis. The addition of the linear gramicidin, another peptide antibiotic synthesized by the same bacterial strain, partially restores transcription by breaking down the tightly packed DNA X peptide complex. The complexed DNA, after nuclease digestion, is retained on a nitrocellulose filter, but loses its affinity for the filter in the presence of gramicidin. The results are discussed with respect to possible functions of the two peptides within in the cell.