ArticleThe Journal of biological chemistry2010
Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 66 citations in OpenAlex.
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- Terrabacteria: redefining bacterial envelope diversity, biogenesis and evolution.Nature reviews. Microbiology · 2025Review
- Cell envelope diversity and evolution across the bacterial tree of life.Nature microbiology · 2024Review
- 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
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- The transmembrane supercomplex mediating the biogenesis of OMPs in Gram-negative bacteria assumes a circular conformational change upon activation.FEBS open bio · 2020Article
- Structural insights into the mechanism of a novel protein targeting pathway in Gram-negative bacteria.FEBS open bio · 2020Article
- Identification of a Compound That Inhibits the Growth of Gram-Negative Bacteria by Blocking BamA-BamD Interaction.Frontiers in microbiology · 2020Article
- Flavin-Based Fluorescent Protein EcFbFP Auto-Guided Surface Display of Methyl Parathion Hydrolase in Escherichia coli.Molecular biotechnology · 2019Article
- The small molecule nitazoxanide selectively disrupts BAM-mediated folding of the outer membrane usher protein.The Journal of biological chemistry · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- The TAM: A Translocation and Assembly Module of the β-Barrel Assembly Machinery in Bacterial Outer Membranes.EcoSal Plus · 2019Review
- A unified model for BAM function that takes into account type Vc secretion and species differences in BAM composition.AIMS microbiology · 2018Article
- Non-peptide guided auto-secretion of recombinant proteins by super-folder green fluorescent protein in Escherichia coli.Scientific reports · 2017Article
- The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Scientific reports · 2016Article
- Polypeptide Transport-Associated Domains of the Toc75 Channel Protein Are Located in the Intermembrane Space of Chloroplasts.Plant physiology · 2016Article
- Cross-species chimeras reveal BamA POTRA and β-barrel domains must be fine-tuned for efficient OMP insertion.Molecular microbiology · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Omp85 proteins are essential proteins located in the bacterial outer membrane. They are involved in outer membrane biogenesis and assist outer membrane protein insertion and folding by an unknown mechanism. Homologous proteins exist in eukaryotes, where they mediate outer membrane assembly in organelles of endosymbiotic origin, the mitochondria and chloroplasts. We set out to explore the homologous relationship between cyanobacteria and chloroplasts, studying the Omp85 protein from the thermophilic cyanobacterium Thermosynechococcus elongatus. Using state-of-the art sequence analysis and clustering methods, we show how this protein is more closely related to its chloroplast homologue Toc75 than to proteobacterial Omp85, a finding supported by single channel conductance measurements. We have solved the structure of the periplasmic part of the protein to 1.97 A resolution, and we demonstrate that in contrast to Omp85 from Escherichia coli the protein has only three, not five, polypeptide transport-associated (POTRA) domains, which recognize substrates and generally interact with other proteins in bigger complexes. We model how these POTRA domains are attached to the outer membrane, based on the relationship of Omp85 to two-partner secretion system proteins, which we show and analyze. Finally, we discuss how Omp85 proteins with different numbers of POTRA domains evolved, and evolve to this day, to accomplish an increasing number of interactions with substrates and helper proteins.
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