A Pathway for Disulfide Bond Formation in vivo

Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its abili...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-02, Vol.90 (3), p.1038-1042
Main Authors: BARDWELL, J. C. A, JIE-OH LEE, JANDER, G, MARTIN, N, BELIN, D, BECKWITH, J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological and medical sciences
Cell membranes
Chemical bonding
Cysteine - metabolism
Cystine - metabolism
disulfide bonds
Disulfides
Disulfides - metabolism
DNA
DsbA protein
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
formation
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetic mutation
Genetics
Isomerases - genetics
Isomerases - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Miscellaneous
Models, Biological
Molecular Sequence Data
Molecules
Mutagenesis
Mutation
Open reading frames
Oxidation
Oxidoreductases - genetics
Oxidoreductases - metabolism
Periplasm
Plasmids
Protein Disulfide-Isomerases
Protein Processing, Post-Translational
Proteins
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its ability to donate its disulfide bond to target proteins. We propose that DsbB, an integral membrane protein, may be involved in transducing redox potential across the cytoplasmic membrane.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.3.1038