ArticleMolecular cell2021
BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.
Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A plasmid toolbox for the easy autodisplay of recombinant proteins and its optimization.Communications biology · 2026Article
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : the preprint server for biology · 2026Article
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- From gatekeepers to mitochondrial mischief: how bacterial outer membrane proteins crash the host cell party.FEMS microbiology reviews · 2026Review
- Engineering non-pathogenic bacteria for auto-transporter-driven secretion of functional interferon.Gut microbes · 2025Article
- Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.Cell surface (Amsterdam, Netherlands) · 2025Article
- Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Article
- Biogenesis of mitochondrial β-barrel membrane proteins.FEBS open bio · 2024Review
- POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane.Nature communications · 2024Article
- ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics.Protein science : a publication of the Protein Society · 2024Review
- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- Article
- In Vivo Disulfide-Bond Crosslinking to Study β-Barrel Membrane Protein Interactions, Dynamicity, and Folding Intermediates.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Surveying membrane landscapes: a new look at the bacterial cell surface.Nature reviews. Microbiology · 2023Review
- Article
- Heterologous Display ofMembranes · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The β-barrel assembly machine (BAM) integrates β-barrel proteins into the outer membrane (OM) of Gram-negative bacteria. An essential BAM subunit (BamA) catalyzes integration by promoting the formation of a hybrid-barrel intermediate state between its own β-barrel domain and that of its client proteins. Here we show that in addition to catalyzing the integration of β-barrel proteins, BamA functions as a polypeptide export channel. In vivo structural mapping via intermolecular disulfide crosslinking showed that the extracellular "passenger" domain of a member of the "autotransporter" superfamily of virulence factors traverses the OM through the BamA β-barrel lumen. Furthermore, we demonstrate that a highly conserved residue within autotransporter β-barrels is required to position the passenger inside BamA to initiate translocation and that during translocation, the passenger stabilizes the hybrid-barrel state. Our results not only establish a new function for BamA but also unify the divergent functions of BamA and other "Omp85" superfamily transporters.
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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.