ArticlePLoS biology2006
Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.
Article in PLoS biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers.
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Who cites it
168 citing papers in PubMed, 323 citations in OpenAlex.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- BAM-BepA complexes in outer membrane protein quality control.Nature communications · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- Targeting of the Gram-Negative Outer Membrane for Antibiotic Discovery and Potentiation.ACS infectious diseases · 2026Review
- 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
- Unveiling the role of outer membrane proteins (OMPs) in biofilm formation and Harnessing them for targeting biofilm-forming bacterial infections.World journal of microbiology & biotechnology · 2026Review
- Analysis of the Kinetics of Folding and Insertion of β-Barrel Membrane Proteins by Gel-Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The dynamic lateral gate of the mitochondrial β-barrel biogenesis machinery is blocked by darobactin A.Nature communications · 2025Article
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Evaluating Cassava Starch Residue as a Maize Substitute in Broiler Chicken Diets.Food science & nutrition · 2025Article
- The discovery and structural basis of two distinct state-dependent inhibitors of BamA.Nature communications · 2024Article
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Discovery and Characterization of Two Folded Intermediates for Outer Membrane Protein TolC Biogenesis.Journal of molecular biology · 2024Article
- The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 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
- Article
- Recombinant Expression and Overproduction of Transmembrane β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
108 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integral beta-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which Omp85 is an evolutionary conserved central component. To study its molecular mechanism, we have produced Omp85 from Escherichia coli in inclusion bodies and refolded it in vitro. The interaction of Omp85 with its substrate proteins was studied in lipid-bilayer experiments, where it formed channels. The properties of these channels were affected upon addition of unfolded outer-membrane proteins (OMPs) or synthetic peptides corresponding to their C-terminal signature sequences. The interaction exhibited species specificity, explaining the inefficient assembly of OMPs from Neisseria in E. coli. Accordingly, the in vivo assembly of the neisserial porin PorA into the E. coli outer membrane was accomplished after adapting its signature sequence. These results demonstrate that the Omp85 assembly machinery recognizes OMPs by virtue of their C-terminal signature sequence.
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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.