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Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes
Author(s) -
van Klompenburg Wim,
Paetzel Mark,
de Jong Joris M.,
Dalbey Ross E.,
Demel Rudy A.,
von Heijne Gunnar,
de Kruijff Ben
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00733-9
Subject(s) - phosphatidylethanolamine , membrane , vesicle , transmembrane domain , chemistry , transmembrane protein , biophysics , inner membrane , membrane protein , biochemistry , bacterial outer membrane , serine , integral membrane protein , escherichia coli , phospholipid , biology , enzyme , receptor , phosphatidylcholine , gene
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.