Identification and characterization of an ATP Binding Cassette L-carnitine transporter in Listeria monocytogenes.

KR Fraser, D Harvie, Peter John Coote, CP O'Byrne

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74 Citations (Scopus)

Abstract

We identified an operon in Listeria monocytogenes EGD with high levels of sequence similarity to the operons encoding the OpuC and OpuB compatible solute transporters from Bacillus subtilis, which are members of the ATP binding cassette (ABC) substrate binding protein-dependent transporter superfamily. The operon, designated opuC, consists of four genes which are predicted to encode an ATP binding protein (OpuCA), an extracellular substrate binding protein (OpuCC), and two membrane-associated proteins presumed to form the permease (OpuCB and OpuCD). The operon is preceded by a potential SigB-dependent promoter, hn opuC-defective mutant was generated by the insertional inactivation of the opuCA gene. The mutant was impaired for growth at high osmolarity in brain heart infusion broth and failed to grow in a defined medium. Supplementation of the defined medium with peptone restored the growth of the mutant in this medium. The mutant was found to accumulate the compatible solutes glycine betaine and choline to same extent as the parent strain but was defective in the uptake of L-carnitine. We conclude that the opuC operon in L. monocytogenes encodes an ABC compatible solute transporter which is capable of transporting L-carnitine and which plays an important role in osmoregulation in this pathogen.

Original languageEnglish
Pages (from-to)4696-4704
Number of pages9
JournalApplied and Environmental Microbiology
Volume66
Publication statusPublished - Nov 2000

Keywords

  • OSMOPROTECTANT GLYCINE BETAINE
  • BACILLUS-SUBTILIS
  • HIGH OSMOLARITY
  • SCOTT-A
  • ABC TRANSPORTERS
  • SYSTEM
  • GROWTH
  • PROTEIN
  • GENE
  • OSMOTOLERANCE

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