Heterologous processing and export of the bacteriocins pediocin PA-1 and lactococcin A in Lactococcus lactis: A study with leader exchange

M. Chikindas, E. Emond, A. J. Haandrikman, J. Kok, K. Leenhouts, S. Pandian, G. Venema, K. Venema

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The bacteriocins pediocin PA-1 and lactococcin A are synthesized as precursors carrying N-terminal extensions with a conserved cleavage site preceded by two glycine residues in positions -2 and -1. Each bacteriocin is translocated through the cytoplasmic membrane by an integral membrane protein of the ABC cassette superfamily which, in the case of pediocin PA-1, has been shown to possess peptidase activity responsible for proteolytic cleavage of the pre-bacteriocin. In each case, another integral membrane protein is essential for bacteriocin production. In this study, a two-step PCR approach was used to permutate the leaders of pediocin PA-1 and lactococcin A. Wild-type and chimeric pre-bacteriocins were assayed for maturation by the processing/export machinery of pediocin PA-1 and lactococcin A. The results show that pediocin PA-1 can be efficiently exported by the lactococcin machinery whether it carries the lactococcin or the pediocin leader. It can also compete with wild-type lactococcin A for the lactococcin machinery. Pediocin PA-1 carrying the lactococcin A leader or lactococcin A carrying that of pediocin PA-1 was poorly secreted when complemented with the pediocin PA-1 machinery, showing that the pediocin machinery is more specific for its bacteriocin substrate. Wild-type pre-pediocin and chimeric pre-pediocin were shown to be processed by the lactococcin machinery at or near the double-glycine cleavage site. These results show the potential of the lactococcin LcnC/LcnD machinery as a maturation system for peptides carrying double-glycine-type amino-terminal leaders.

Original languageEnglish (US)
Pages (from-to)66-76
Number of pages11
JournalProbiotics and Antimicrobial Proteins
Volume2
Issue number2
DOIs
StatePublished - Jun 2010

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Medicine
  • Molecular Biology

Keywords

  • Bacteriocin
  • Double-glycine leader
  • Lactococcin
  • Pediocin

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