ArticleApplied and environmental microbiology2012
Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Synthetic anti-RNA antibody derivatives for RNA visualization in mammalian cells.Nucleic acids research · 2025Article
- Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.Nature communications · 2020Article
- Antibacterial activity and mechanism of action of auranofin against multi-drug resistant bacterial pathogens.Scientific reports · 2016Article
- Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.Molecular cell · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli β-galactosidase is probably the most widely used reporter enzyme in molecular biology, cell biology, and biotechnology because of the easy detection of its activity. Its large size and tetrameric structure make this bacterial protein an interesting model for crystallographic studies and atomic mapping. In the present study, we investigate a version of Escherichia coli β-galactosidase produced under oxidizing conditions, in the cytoplasm of an Origami strain. Our data prove the activation of this microbial enzyme under oxidizing conditions and clearly show the occurrence of a disulfide bond in the β-galactosidase structure. Additionally, the formation of this disulfide bond is supported by the analysis of a homology model of the protein that indicates that two cysteines located in the vicinity of the catalytic center are sufficiently close for disulfide bond formation.
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