pH-induced insertion of the amphiphilic alpha-helical anchor of Escherichia coli penicillin-binding protein 5.
By treating vesicles prepared from Escherichia coli K12 with various reagents, we have investigated the mechanism by which penicillin-binding protein 5 anchors to the inner membrane. The results indicate that there are two forms of anchoring; one which is inaccessible to urea and probably inserted into the bilayer and one which is accessible. Association of the accessible form with the membrane seems to involve significant hydrophobic interaction and this form is triggered to undergo reversible 'insertion' by a decrease in pH.
Department of Biochemistry, University of Liverpool, England.
D A
DA
Phoenix
J M
JM
Pratt
D001426:Bacterial Proteins; D001665:Binding Sites / Q000187:drug effects / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006602:Hexosyltransferases; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers / Q000378:metabolism; D008954:Models, Biological; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D014508:Urea / Q000494:pharmacology
D001426:Bacterial Proteins; D002352:Carrier Proteins; D008051:Lipid Bilayers; D046915:Penicillin-Binding Proteins; D014508:Urea; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase