pH‐Induced insertion of the amphiphilic α‐helical anchor of Escherichia coli penicillin‐binding protein 5
- 1 June 1990
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 190 (2) , 365-369
- https://doi.org/10.1111/j.1432-1033.1990.tb15584.x
Abstract
By treating vesicles prepared from Excherichia coli K12 with various reagents, we have investigated the mechanism by which peicillin-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.Keywords
This publication has 17 references indexed in Scilit:
- Analysis of the membrane‐binding domain of penicillin‐binding protein 5 of Escherichia coliMolecular Microbiology, 1988
- An 18 amino acid amphiphilic helix forms the membrane‐anchoring domain of the Escherichia coli penicillin‐binding protein 5Molecular Microbiology, 1987
- Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes.Proceedings of the National Academy of Sciences, 1985
- Analysis of membrane and surface protein sequences with the hydrophobic moment plotJournal of Molecular Biology, 1984
- An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin‐binding protein 5 of Escherichia coliFEBS Letters, 1984
- Regulation of the synthesis of surface protein in the cell cycle of e. coli b/rCell, 1979
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Use of Helical Wheels to Represent the Structures of Proteins and to Identify Segments with Helical PotentialBiophysical Journal, 1967