Bioengineering of lanthipeptides in Escherichia coli: assessing the specificity of lichenicidin and haloduracin biosynthetic machinery

T. Caetano*, J. Barbosa, E. Möesker, R. D. Süssmuth, S. Mendo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

The lichenicidin and haloduracin biosynthetic machinery specificity was investigated invivo in Escherichia coli. Unlike previous reports using different hosts, it was found that the biosynthetic machineries of lichenicidin and haloduracin are highly specific to their dedicated peptide precursors. Likewise, the substitution of lichenicidin structural genes by chimeras of lichenicidin leader sequences and haloduracin core peptides did not yield mature haloduracin peptides. Despite these restrictions, it was found that the bifunctional enzyme HalT was able to process and export lichenicidin peptides. These findings corroborate the promiscuity of LanT enzymes reported for other lantibiotics, such as nukacin ISK-1 and lacticin 481.
Original languageEnglish
Pages (from-to)600-604
Number of pages5
JournalResearch in Microbiology
Volume165
Issue number7
DOIs
Publication statusPublished - 2014
Externally publishedYes

Keywords

  • Bacillus
  • Bacteriocins
  • Chimeras
  • Invivo
  • Lantibiotics

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