Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE

Biosci Biotechnol Biochem. 2009 Oct;73(10):2310-6. doi: 10.1271/bbb.90451. Epub 2009 Oct 7.


The LolCDE complex is an ATP-binding cassette transporter that mediates the release of newly synthesized lipoproteins from the cytoplasmic membrane of gram-negative bacteria, which results in the initiation of outer-membrane sorting of lipoproteins through the Lol pathway. LolCDE is composed of one copy each of membrane subunits LolC and LolE, and two copies of nucleotide-binding subunit LolD. In this study, we examined the membrane topology of LolC and LolE by PhoA fusion analysis. Both LolC and LolE were found to have four transmembrane segments with a large periplasmic loop exposed to the periplasm. Despite similarities in sequence and topology, the accessibility of a sulfhydryl reagent to Cys introduced into the periplasmic loop suggested that the structure of the periplasmic region differs between LolC and LolE. Inhibition of the release of lipoproteins by the sulfhydryl reagent supported a previous proposal that LolC and LolE have distinct functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / metabolism*
  • Amino Acid Sequence
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism*
  • Cysteine / metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Lipoproteins / metabolism
  • Molecular Sequence Data
  • Periplasm / chemistry
  • Periplasm / metabolism*
  • Sulfonic Acids / chemistry
  • Sulfonic Acids / metabolism


  • ATP-Binding Cassette Transporters
  • Escherichia coli Proteins
  • Lipoproteins
  • LolC protein, E coli
  • LolE protein, E coli
  • Sulfonic Acids
  • Cysteine