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Article

Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering.

The Journal of biological chemistry - 7 Oct 1994

Duché D, Baty D, Chartier M, Letellier L

Abstract excerpt

Three double cysteine mutants, each possessing a disulfide bond in its pore-forming domain, were used to study the translocation of colicin A through the Escherichia coli envelope. These mutated colicins were able to exert their in vivo channel activity only after their disulfide bonds had been reduced by dithiothreitol. In solution, the reduction of the disulfide bonds by dithiothreitol was a slow process whose...

Topics

Bacterial Outer Membrane Proteins
Biological Transport
Colicins
Disulfides
Dithiothreitol
Escherichia coli
Escherichia coli Proteins
Membrane Transport Proteins
Mutation
Protein Folding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Peptide

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Identifiers

PMID: 7929161

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7929161-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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