An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals

FEBS Lett. 2006 Feb 13;580(4):1164-70. doi: 10.1016/j.febslet.2005.10.038. Epub 2005 Nov 2.

Abstract

Bacterial lipoproteins are anchored to membranes through a lipid moiety attached to the N-terminal Cys. Escherichia coli possesses more than 90 species of lipoproteins, most of which are localized in the outer membrane and others in the inner membrane. Sorting of lipoproteins to the outer membrane requires the Lol system comprising five Lol proteins. An ATP-binding cassette transporter, LolCDE, initiates the lipoprotein sorting by mediating the detachment of outer membrane-specific lipoproteins from the inner membrane. LolCDE does not recognize lipoproteins possessing Asp at position 2, which therefore remain anchored to the inner membrane. We will discuss the mechanism of LolCDE based on data obtained through in vitro experiments.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / physiology*
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Bacterial Adhesion / physiology*
  • Hydrolysis
  • Lipoproteins / physiology
  • Molecular Sequence Data
  • Protein Sorting Signals*
  • Sequence Homology, Amino Acid

Substances

  • ATP-Binding Cassette Transporters
  • Lipoproteins
  • Protein Sorting Signals
  • Adenosine Triphosphate