Membrane topology of the lactococcal bacteriocin ATP-binding cassette transporter protein LcnC: Involvement of LcnC in lactococcin A maturation

CM Franke, J Tiemersma, G Venema, J Kok*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

37 Citations (Scopus)

Abstract

Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors with N-terminal leader peptides different from those present in preproteins exported by the general sec-dependent (type II) secretion pathway. These bacteriocins utilize a dedicated (type I) secretion system for externalization. The secretion apparatus for the lactococcins A, B, and M/N (LcnA, B, and M/N) from Lactococcus lactis is composed of the two membrane proteins LcnC and LcnD, LcnC belongs to the ATP-binding cassette transporters, whereas LcnD is a protein with similarities to other accessory proteins of type I secretion systems, This paper shows that the N-terminal part of LcnC is involved in the processing of the precursor of LcnA By making translational fusions of LcnC to the reporter proteins beta-galactosidase (LacZ) and alkaline phosphatase (PhoA*), it was shown that both the N- and C-terminal parts of LcnC are located in the cytoplasm, As the N terminus of LcnC is required for LcnA maturation and is localized in the cytoplasm, we conclude that the processing of the bacteriocin LcnA to its mature form takes place at the cytosolic side of the cytoplasmic membrane.

Original languageEnglish
Pages (from-to)8484-8490
Number of pages7
JournalThe Journal of Biological Chemistry
Volume274
Issue number13
DOIs
Publication statusPublished - 26-Mar-1999

Keywords

  • LACTIS SUBSP LACTIS
  • ESCHERICHIA-COLI
  • STREPTOCOCCUS-LACTIS
  • ALKALINE-PHOSPHATASE
  • P-GLYCOPROTEIN
  • ABC TRANSPORTERS
  • IMMUNITY PROTEIN
  • CLONING VECTORS
  • PLASMID
  • FUSION

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