Journal article
PagP Activation in the Outer Membrane Triggers R3 Core Oligosaccharide Truncation in the Cytoplasm of Escherichia coli O157:H7*
Abstract
The Escherichia coli outer membrane phospholipid:lipid A palmitoyltransferase PagP is normally a latent enzyme, but it can be directly activated in outer membranes by lipid redistribution associated with a breach in the permeability barrier. We now demonstrate that a lipid A myristate deficiency in an E. coli O157:H7 msbB mutant constitutively activates PagP in outer membranes. The lipid A myristate deficiency is associated with hydrophobic …
Authors
Smith AE; Kim S-H; Liu F; Jia W; Vinogradov E; Gyles CL; Bishop RE
Journal
Journal of Biological Chemistry, Vol. 283, No. 7, pp. 4332–4343
Publisher
Elsevier
Publication Date
February 2008
DOI
10.1074/jbc.m708163200
ISSN
0021-9258
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AcyltransferasesBase SequenceCarbohydrate ConformationCarbohydrate SequenceCatalysisCytoplasmDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coli O157Escherichia coli ProteinsMicrobial Sensitivity TestsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularOligosaccharidesSpectrometry, Mass, Electrospray Ionization