ArticleNature communications2017
Folding of a bacterial integral outer membrane protein is initiated in the periplasm.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The trial behind it
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
29 citing papers in PubMed, 46 citations in OpenAlex.
- Insights into the complex formation of a trimeric autotransporter adhesin with a peptidoglycan-binding periplasmic protein.Cell surface (Amsterdam, Netherlands) · 2025Article
- A periplasmic zinc capture protein enhances the resistance ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Article
- 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
- 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
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- Simple But Efficacious Enrichment of Integral Membrane Proteins and Their Interactions for In-Depth Membrane Proteomics.Molecular & cellular proteomics : MCP · 2022Article
- Overproducing the BAM complex improves secretion of difficult-to-secrete recombinant autotransporter chimeras.Microbial cell factories · 2021Article
- Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes.mBio · 2021Article
- Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021Review
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.mBio · 2021Article
- The assembly of β-barrel outer membrane proteins.Current opinion in microbiology · 2021Review
- Coaggregation properties of trimeric autotransporter adhesins.MicrobiologyOpen · 2020Article
- BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020Article
- Article
- Recent advances in the understanding of trimeric autotransporter adhesins.Medical microbiology and immunology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Bam complex promotes the insertion of β-barrel proteins into the bacterial outer membrane, but it is unclear whether it threads β-strands into the lipid bilayer in a stepwise fashion or catalyzes the insertion of pre-folded substrates. Here, to distinguish between these two possibilities, we analyze the biogenesis of UpaG, a trimeric autotransporter adhesin (TAA). TAAs consist of three identical subunits that together form a single β-barrel domain and an extracellular coiled-coil ("passenger") domain. Using site-specific photocrosslinking to obtain spatial and temporal insights into UpaG assembly, we show that UpaG β-barrel segments fold into a trimeric structure in the periplasm that persists until the termination of passenger-domain translocation. In addition to obtaining evidence that at least some β-barrel proteins begin to fold before they interact with the Bam complex, we identify several discrete steps in the assembly of a poorly characterized class of virulence factors.
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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.