Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence

C Kaletta1, K D Entian, R Kellner

  • 1Institut für Mikrobiologie, Universität Frankfurt, Federal Republic of Germany.

Archives of Microbiology
|January 1, 1989
PubMed

Insights

Researchers identified the lantibiotic Pep5 gene (pepA) on plasmid pED503 using a synthetic oligonucleotide probe. This confirms Pep5 is ribosomally synthesized and reveals details about its prepeptide structure and maturation process.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Lantibiotics are ribosomally synthesized peptides with antimicrobial properties.
  • Pep5 is a lantibiotic whose genetic basis and maturation pathway were previously uncharacterized.

Purpose of the Study:

  • To identify and characterize the structural gene (pepA) for the lantibiotic Pep5.
  • To elucidate the ribosomal synthesis and maturation process of Pep5.

Main Methods:

  • Oligonucleotide probe design based on the Pep5 propeptide sequence.
  • Hybridization screening to locate the pepA gene on plasmid pED503.
  • Nucleotide sequencing of the pepA gene.

Main Results:

  • The structural gene pepA was identified on the 18.6 kbp plasmid pED503.
  • Nucleotide sequencing revealed pepA codes for a 60-residue prepeptide, confirming ribosomal synthesis.
  • The prepeptide N-terminus exhibits alpha-helix probability, with a cleavage site preceding the 34-residue propeptide.

Conclusions:

  • Pep5 is confirmed to be ribosomally synthesized.
  • The maturation of Pep5 likely involves enzymatic modification of amino acids and proteolytic cleavage.
  • A model for Pep5 maturation includes dehydration, sulfide bridge formation, translocation, and cleavage.

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