Pathways of disulfide bond formation in Escherichia coli.

TitlePathways of disulfide bond formation in Escherichia coli.
Publication TypeJournal Article
Year of Publication2006
AuthorsMessens, J., and J-F. Collet
JournalInt J Biochem Cell Biol
Volume38
Issue7
Pagination1050-62
Date Published2006
Type of Articleredox
ISSN1357-2725
KeywordsAmino Acid Sequence, Animals, Bacterial Proteins, Catalysis, Cysteine, Dimerization, Disulfides, Endoplasmic Reticulum, Escherichia coli, Membrane Proteins, Models, Molecular, Molecular Structure, Oxidation-Reduction, Protein Conformation, Protein Disulfide-Isomerases, Protein Folding, Thioredoxins
Abstract

Disulfide bond formation is required for the correct folding of many secreted proteins. Cells possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are joined during the folding process. These enzymatic systems are located in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model.
DOI10.1016/j.biocel.2005.12.011
Alternate JournalInt. J. Biochem. Cell Biol.
PubMed ID16446111
subject_category: 
Redox
Research group: 
MessensGroup