ArticleProceedings of the National Academy of Sciences of the United States of America2013
Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.
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 59 papers.
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Who cites it
59 citing papers in PubMed.
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- First inhibitor of a bacterial two-partner secretion system.bioRxiv : the preprint server for biology · 2026Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Outer membrane protein assembly mediated by BAM-SurA complexes.Nature communications · 2024Article
- 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
- In Vivo Site-Directed and Time-Resolved Photocrosslinking of Envelope Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- BamE directly interacts with BamA and BamD coordinating their functions.Molecular microbiology · 2023Article
- Uncovering the folding mechanism of pertactin: A comparative study of isolated and vectorial folding.Biophysical journal · 2023Article
- Small Molecule Antibiotics Inhibit Distinct Stages of Bacterial Outer Membrane Protein Assembly.mBio · 2022Article
- Article
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Nature communications · 2021Article
- High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- The assembly of β-barrel membrane proteins by BAM and SAM.Molecular microbiology · 2021Review
- Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.Journal of bacteriology · 2020Article
- The gain-of-function alleleProceedings of the National Academy of Sciences of the United States of America · 2020Article
- BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020Article
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Authors and funding
4 authors.
Funding
Abstract
Autotransporters are bacterial virulence factors that contain an N-terminal extracellular ("passenger") domain and a C-terminal β barrel ("β") domain that anchors the protein to the outer membrane. The β domain is required for passenger domain secretion, but its exact role in autotransporter biogenesis is unclear. Here we describe insights into the function of the β domain that emerged from an analysis of mutations in the Escherichia coli O157:H7 autotransporter EspP. We found that the G1066A and G1081D mutations slightly distort the structure of the β domain and delay the initiation of passenger domain translocation. Site-specific photocrosslinking experiments revealed that the mutations slow the insertion of the β domain into the outer membrane, but do not delay the binding of the β domain to the factor that mediates the insertion reaction (the Bam complex). Our results demonstrate that the β domain does not simply target the passenger domain to the outer membrane, but promotes translocation when it reaches a specific stage of assembly. Furthermore, our results provide evidence that the Bam complex catalyzes the membrane integration of β barrel proteins in a multistep process that can be perturbed by minor structural defects in client proteins.
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