In vivo function and membrane binding properties are correlated for Escherichia coli lamB signal peptides

Science. 1985 May 31;228(4703):1096-9. doi: 10.1126/science.3158076.


Wild-type and pseudorevertant signal peptides of the lamB gene product of Escherichia coli interact with lipid systems whereas a nonfunctional deletion mutant signal peptide does not. This conclusion is based on interaction of synthetic signal peptides with a lipid monolayer-water surface, conformational changes induced by presence of lipid vesicles in an aqueous solution of signal peptide, and capacities of the peptides to promote vesicle aggregation. Analysis of the signal sequences and previous conformational studies suggest that these lipid interaction properties may be attributable to the tendency of the functional signal peptides to adopt alpha-helical conformations. Although the possibility of direct interaction between the signal peptide and membrane lipids during protein secretion is controversial, the results suggest that conformationally related amphiphilicity and consequent membrane affinity of signal sequences are important for function in vivo.

Publication types

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

MeSH terms

  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacteriophage lambda / metabolism
  • Biological Transport
  • Chemical Phenomena
  • Chemistry, Physical
  • Circular Dichroism
  • Membrane Lipids / metabolism
  • Models, Biological
  • Peptides / metabolism*
  • Phospholipids / metabolism*
  • Porins
  • Protein Conformation
  • Protein Sorting Signals
  • Receptors, Virus / metabolism*
  • Structure-Activity Relationship
  • Surface Properties
  • Water


  • Bacterial Outer Membrane Proteins
  • Membrane Lipids
  • Peptides
  • Phospholipids
  • Porins
  • Protein Sorting Signals
  • Receptors, Virus
  • maltoporins
  • Water