ArticleProceedings of the National Academy of Sciences of the United States of America2013
Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- The Love and Hate Relationship between T5SS and Other Secretion Systems in Bacteria.International journal of molecular sciences · 2023Pooled it
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- Uncovering the folding mechanism of pertactin: A comparative study of isolated and vectorial folding.Biophysical journal · 2023Article
- Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Recent advances in the understanding of trimeric autotransporter adhesins.Medical microbiology and immunology · 2020Review
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- Article
- The Rich Tapestry of Bacterial Protein Translocation Systems.The protein journal · 2019Review
- Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel.Nature communications · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Type V Secretion Systems: An Overview of Passenger Domain Functions.Frontiers in microbiology · 2019Review
- Identification of a novel post-insertion step in the assembly of a bacterial outer membrane protein.Molecular microbiology · 2018Article
- A unified model for BAM function that takes into account type Vc secretion and species differences in BAM composition.AIMS microbiology · 2018Article
- A lower isoelectric point increases signal sequence-mediated secretion of recombinant proteins through a bacterial ABC transporter.The Journal of biological chemistry · 2017Article
- Folding of a bacterial integral outer membrane protein is initiated in the periplasm.Nature communications · 2017Article
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
- 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
- A nanobody:GFP bacterial platform that enables functional enzyme display and easy quantification of display capacity.Microbial cell factories · 2016Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Autotransporters are a large class of virulence proteins produced by Gram-negative bacteria. They contain an N-terminal extracellular ("passenger") domain that folds into a β-helical structure and a C-terminal β-barrel ("β") domain that anchors the protein to the outer membrane. Because the periplasm lacks ATP, the source of energy that drives passenger domain secretion is unknown. The prevailing model postulates that vectorial folding of the β-helix in the extracellular space facilitates unidirectional secretion of the passenger domain. In this study we used a chimeric protein composed of the 675-residue receptor-binding domain (RD) of the Bordetella pertussis adenylate cyclase toxin CyaA fused to the C terminus of the Escherichia coli O157:H7 autotransporter EspP to test this hypothesis. The RD is a highly acidic, repetitive polypeptide that is intrinsically disordered in the absence of calcium. Surprisingly, we found that the RD moiety was efficiently secreted when it remained in an unfolded conformation. Furthermore, we found that neutralizing or reversing the charge of acidic amino acid clusters stalled translocation in the vicinity of the altered residues. These results challenge the vectorial folding model and, together with the finding that naturally occurring passenger domains are predominantly acidic, provide evidence that a net negative charge plays a significant role in driving the translocation reaction.
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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.