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Area of Science:

  • Natural Product Chemistry
  • Microbiology
  • Biochemistry

Background:

  • Linaridins and lanthipeptides are distinct classes within the ribosomally synthesized and posttranslationally modified peptide (RiPP) superfamily.
  • Both RiPP classes share structural features like dehydroamino acids and thioether cross-links, but utilize different enzymatic pathways for biosynthesis.
  • Previous understanding suggested specific biosynthetic pathways for linaridins and lanthipeptides.

Purpose of the Study:

  • To identify and characterize novel RiPPs from Streptomyces lividans.
  • To elucidate the structural and functional differences between linaridins and lanthipeptides.
  • To investigate the role of specific structural moieties in antimicrobial activity.

Main Methods:

  • Recombinant expression of the cypemycin biosynthetic gene cluster in Streptomyces lividans.
  • Extensive structural analysis, including determination of stereochemistry for amino acids.
  • Genetic manipulation (knockout and mutagenesis) to study gene function.
  • Comparative analysis of cypepeptin and cypemycin structures and activities.

Main Results:

  • Identification of a novel lanthipeptide, cypepeptin, from a modified Streptomyces lividans strain.
  • Discovery of multiple d-amino acids and Z-dehydrobutyrines in both cypepeptin and cypemycin, challenging previous structural assumptions.
  • The aminovinyl-cysteine (AviCys) moiety in cypemycin was found essential for disrupting Micrococcus luteus cell integrity.
  • The lanthionine moiety in cypepeptin could not functionally replace the AviCys moiety's cell-disrupting activity.

Conclusions:

  • Cypepeptin represents a novel lanthipeptide with unique structural features.
  • The presence of d-amino acids and Z-dehydrobutyrines is more widespread in these RiPP classes than previously thought.
  • The AviCys modification in cypemycin is critical for its specific antimicrobial mechanism, highlighting structure-function relationships in RiPPs.