A single amino acid determinant of the membrane localization of lipoproteins in E. coli

Cell. 1988 May 6;53(3):423-32. doi: 10.1016/0092-8674(88)90162-6.

Abstract

When beta-lactamase was fused with the signal peptide plus the amino-terminal 9 amino acid residues of the major outer membrane lipoprotein, the resultant lipo-beta-lactamase (LL-1) was shown to be localized to the outer membrane. However, when the 9 residue sequence was replaced with the amino-terminal 12 residue sequence of lipoprotein-28, an inner membrane protein, the resultant lipo-beta-lactamase (LL-2) was found exclusively in the inner membrane. The localization of LL-2 was shifted to the outer membrane simply by substituting the second amino acid residue (Asp) of LL-2 with Ser. Conversely, the alteration of the second residue (Ser) of LL-1 to Asp resulted in the localization of LL-1 to the inner membrane. These results suggest that the second amino acid residue of the lipoproteins plays a crucial role in determining their final locations in the E. coli envelope.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / analysis
  • Centrifugation, Density Gradient
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / analysis*
  • Escherichia coli / genetics
  • Escherichia coli / ultrastructure
  • Lipoproteins / analysis*
  • Lipoproteins / genetics
  • Membrane Proteins / analysis*
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Mutation
  • Plasmids
  • Protein Sorting Signals / analysis
  • Protein Sorting Signals / genetics
  • Protein Sorting Signals / physiology
  • Recombinant Fusion Proteins / analysis
  • Recombinant Fusion Proteins / genetics
  • beta-Lactamases / analysis
  • beta-Lactamases / genetics

Substances

  • Lipoproteins
  • Membrane Proteins
  • Protein Sorting Signals
  • Recombinant Fusion Proteins
  • beta-Lactamases