ArticleJournal of molecular biology2024
Discovery and Characterization of Two Folded Intermediates for Outer Membrane Protein TolC Biogenesis.
Article in Journal of molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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
3 citing papers in PubMed.
- Chemical inhibition of a CBASS anti-bacteriophage defense.iScience · 2026Article
- A historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.npj antimicrobials and resistance · 2025Review
- A robust protocol for refolding TolC and other outer membrane components of tripartite efflux pumps from inclusion bodies.Methods in enzymology · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
TolC is the outer membrane protein responsible for antibiotic efflux in E. coli. Compared to other outer membrane proteins it has an unusual fold and has been shown to fold independently of commonly used periplasmic chaperones, SurA and Skp. Here we find that the assembly of TolC involves the formation of two folded intermediates using circular dichroism, gel electrophoresis, site-specific disulfide bond formation and radioactive labeling. First the TolC monomer folds, and then TolC assembles into a trimer both in detergent-free buffer and in the presence of detergent micelles. We find that a TolC trimer also forms in the periplasm and is present in the periplasm before it inserts in the outer membrane. The monomeric and trimeric folding intermediates may be used in the future to develop a new approach to antibiotic efflux pump inhibition by targeting the assembly pathway of TolC.
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Registered trials
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