Sorting and membrane localization of E.coli lipoproteins

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E.coli lipoproteins are sorted to the outer membrane depending on the amino acid residue located next to the amino-terminal lipid-attached cysteine. The sorting is mediated by the Lol system composed of five Lol proteins. The lipoprotein transfer reaction from LolA to LolB is unidirectional and requires no energy. This reaction was found to depend on the strength of hydrophobic interaction between lipoproteins and LolA or LolB. If the LolA-lipoprotein interaction is too strong, the transfer of lipoprotein to LolB is inhibited. Opening and closing of the hydrophobic cavity of LolA was found to be critical for the LolA function. Finally, the region of LolD important for the interaction with membrane subunits LolC and LolE was determined.