Induction of non-bilayer lipid structures by functional signal peptides.
Using 31P NMR and freeze-fracture electron microscopy we investigated the effect of several synthetic signal peptides on lipid structure in model membranes mimicking the lipid composition of the Escherichia coli inner membrane. It is demonstrated that the signal peptide of the E. coli outer membrane protein PhoE, as well as that of the M13 phage coat protein, strongly promote the formation of non-bilayer lipid structures. This effect appears to be correlated to in vivo translocation efficiency, since a less functional analogue of the PhoE signal peptide was found to be less active in destabilizing the bilayer. It is proposed that signal sequences can induce local changes in lipid structure that are involved in protein translocation across the membrane.
Killian
J A
JA
Centre for Biomembranes and Lipid Enzymology, University of Utrecht, The Netherlands.
de Jong
A M
AM
Bijvelt
J
J
Verkleij
A J
AJ
de Kruijff
B
B
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000032:analysis* / Q000648:ultrastructure; D004926:Escherichia coli / Q000032:analysis; D005614:Freeze Fracturing / Q000379:methods; D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008563:Membrane Lipids / Q000302:isolation & purification; D008567:Membranes, Artificial; D008854:Microscopy, Electron / Q000379:methods; D008969:Molecular Sequence Data; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D010758:Phosphorus; D021382:Protein Sorting Signals / Q000378:metabolism*
D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D008563:Membrane Lipids; D008567:Membranes, Artificial; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D021382:Protein Sorting Signals; C006065:We 201; D010758:Phosphorus; C051388:1,2-dioleoyl-sn-glycero-3-phosphoglycerol; C020888:1,2-dielaidoylphosphatidylethanolamine