ArticleThe Journal of biological chemistry2013
Stepwise folding of an autotransporter passenger domain is not essential for its secretion.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 20 citations in OpenAlex.
- Construction and characterization of a nanopore derived from the transmembrane domain of a trimeric autotransporter adhesin.Frontiers in bioengineering and biotechnology · 2026Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Secretion of the Intimin Passenger Domain Is Driven by Protein Folding.The Journal of biological chemistry · 2016Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
- Extracellular protease digestion to evaluate membrane protein cell surface localization.Nature protocols · 2015Article
- Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Molecular microbiology · 2015Review
- Multiple driving forces required for efficient secretion of autotransporter virulence proteins.The Journal of biological chemistry · 2015Article
- The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.The Journal of biological chemistry · 2015Article
- Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Autotransporters are a superfamily of virulence proteins produced by Gram-negative bacteria. They consist of an N-terminal β-helical domain ("passenger domain") that is secreted into the extracellular space and a C-terminal β-barrel domain ("β-domain") that anchors the protein to the outer membrane. Because the periplasm lacks ATP, vectorial folding of the passenger domain in a C-to-N-terminal direction has been proposed to drive the secretion reaction. Consistent with this hypothesis, mutations that disrupt the folding of the C terminus of the passenger domain of the Escherichia coli O157:H7 autotransporter EspP have been shown to cause strong secretion defects. Here, we show that point mutations introduced at specific locations near the middle or N terminus of the EspP β-helix that perturb folding also impair secretion, but to a lesser degree. Surprisingly, we found that even multiple mutations that potentially abolish the stability of several consecutive rungs of the β-helix only moderately reduce secretion efficiency. Although these results provide evidence that the free energy derived from passenger domain folding contributes to secretion efficiency, they also suggest that a significant fraction of the energy required for secretion is derived from another source.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.