ArticleProceedings of the National Academy of Sciences of the United States of America2005
An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.
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Who cites it
77 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.
- The Love and Hate Relationship between T5SS and Other Secretion Systems in Bacteria.International journal of molecular sciences · 2023Pooled it
- Bacterial serine protease EspP induces differentiation and expansion of enteroendocrine cells in human colonoids.Physiological genomics · 2026Article
- A modular biodevice assembly tool kit for combinatorial screening and benchmarking multiple cell surface display platforms in Escherichia coli.Journal of biological engineering · 2026Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Multiplex, multimodal mapping of variant effects in secreted proteins.bioRxiv : the preprint server for biology · 2025Article
- Decoding the genomic terrain: functional insights into 14 chemosensory proteins in whitefly Bemisia tabaci Asia II-1.Scientific reports · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- Elucidation of ejaculatory bulb proteins in Bemisia tabaci Asia-1 and Asia II-1 and confirmation of their mating transfer via RNAi.Molecular biology reports · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- The Trimeric Autotransporter Adhesin EmaA and Infective Endocarditis.Pathogens (Basel, Switzerland) · 2024Review
- Small Molecule Antibiotics Inhibit Distinct Stages of Bacterial Outer Membrane Protein Assembly.mBio · 2022Article
- Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.mBio · 2021Article
- Antennal Enriched Odorant Binding Proteins Are Required for Odor Communication inBiomolecules · 2021Article
- Cell-free synthesis of the hirudin variant 1 of the blood-sucking leech Hirudo medicinalis.Scientific reports · 2020Article
- Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel.Nature communications · 2019Article
- Review
- Type V Secretion Systems: An Overview of Passenger Domain Functions.Frontiers in microbiology · 2019Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial autotransporters are proteins that use a C-terminal porin-like domain to facilitate the transport of an upstream "passenger domain" across the outer membrane. Although autotransporters are translocated across the inner membrane (IM) via the Sec pathway, some of them contain exceptionally long signal peptides distinguished by a unique N-terminal sequence motif. In this study, we used the Escherichia coli O157:H7 autotransporter EspP as a model protein to investigate the function of the unusual signal peptides. We found that removal of the N-terminal motif or replacement of the EspP signal peptide did not affect translocation of the protein across the IM. Remarkably, modification of the signal peptide caused EspP to misfold in the periplasm and blocked transport of the passenger domain across the outer membrane. Further analysis suggested that the EspP signal peptide transits slowly through the Sec machinery. Based on these results, we propose that the unusual signal peptides not only function as targeting signals, but also prevent misfolding of the passenger domain in the periplasm by transiently tethering it to the IM.
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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.