Open AccesspH‐Induced insertion of the amphiphilic α‐helical anchor of Escherichia coli penicillin‐binding protein 5
Author(s) -
PHOENIX David A.,
PRATT Julie M.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb15584.x
Subject(s) - escherichia coli , chemistry , amphiphile , penicillin binding proteins , bilayer , biophysics , urea , membrane , vesicle , reagent , biochemistry , biology , copolymer , organic chemistry , gene , polymer
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.