pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----Lys.

doi:10.1073/pnas.89.13.6202

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Article

pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----Lys.

Proceedings of the National Academy of Sciences of the United States of America - 1 Jul 1992

O'Keefe D O, Cabiaux V, Choe S, Eisenberg D, Collier R J

Abstract excerpt

To investigate how diphtheria toxin (DT) undergoes pH-dependent membrane translocation in mammalian cells, we have isolated and characterized mutants of the toxin that are defective in acidic-pH-dependent killing of Escherichia coli. Cloned DT secreted to the periplasm of E. coli kills the bacteria under acidic conditions (near pH 5.0) by inserting into and permeabilizing the inner membrane (a mechanism...

Topics

Animals
Biological Transport
Cell Membrane
DNA Mutational Analysis
Diphtheria Toxin
Glutamates
Hydrogen-Ion Concentration
In Vitro Techniques
Lysine
Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Biosynthesis

Protein Conformation

Recombinant Proteins

Structure-Activity Relationship

Vero Cells

Source

Open in PubMed Open full text

Identifiers

PMID: 1631109
DOI: 10.1073/pnas.89.13.6202
PMCID: PMC402150

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1631109-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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