An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals.
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.
Narita
Shin-ichiro
S
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Tokyo 113-0032, Japan.
Tokuda
Hajime
H
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000502:physiology*; D006868:Hydrolysis; D008074:Lipoproteins / Q000502:physiology; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals; D017386:Sequence Homology, Amino Acid
D018528:ATP-Binding Cassette Transporters; D008074:Lipoproteins; D021382:Protein Sorting Signals; D000255:Adenosine Triphosphate