1. Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes
- Author
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Joris de Jong, Wim van Klompenburg, Rudy A. Demel, Ross E. Dalbey, Ben de Kruijff, Gunnar von Heijne, and Mark Paetzel
- Subjects
Signal peptide ,Leader peptidase ,Lipid Bilayers ,Molecular Sequence Data ,Biophysics ,Biochemistry ,Catalysis ,chemistry.chemical_compound ,Membrane Lipids ,Structural Biology ,Genetics ,Escherichia coli ,Inner membrane ,Protein–lipid interaction ,Amino Acid Sequence ,Insertion ,Molecular Biology ,Integral membrane protein ,Phosphatidylethanolamine ,Binding Sites ,Chemistry ,Phosphatidylethanolamines ,Cell Membrane ,Serine Endopeptidases ,Membrane Proteins ,Biological Transport ,Cell Biology ,Transmembrane protein ,Protein-lipid interaction ,Membrane ,Membrane protein ,Protein secretion ,Protein Binding - Abstract
Leader peptidase is an integral membrane protein of E. coli and it catalyses the removal of most signal peptides from translocated precursor proteins. In this study it is shown that when the transmembrane anchors are removed in vivo, the remaining catalytic domain can bind to inner and outer membranes of E. coli. Furthermore, the purified catalytic domain binds to inner membrane vesicles and vesicles composed of purified inner membrane lipids with comparable efficiency. It is shown that the interaction is caused by penetration of a part of the catalytic domain between the lipids. Penetration is mediated by phosphatidylethanolamine, the most abundant lipid in E. coli, and does not seem to depend on electrostatic interactions. A hydrophobic segment around the catalytically important residue serine 90 is required for the interaction with membranes.
- Published
- 1998