ArticleProceedings of the National Academy of Sciences of the United States of America2017
Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- 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
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Exploring the Terra incognita of AI-based domain classifications.Protein science : a publication of the Protein Society · 2025Article
- Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 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
- Recombinant Expression and Overproduction of Transmembrane β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- The assembly of β-barrel outer membrane proteins.Current opinion in microbiology · 2021Review
- The gain-of-function alleleProceedings of the National Academy of Sciences of the United States of America · 2020Article
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- Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel.Nature communications · 2019Article
- Fine-Tuning of σJournal of bacteriology · 2019Article
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.Nature communications · 2018Article
- Inhibitor of intramembrane protease RseP blocks the σProceedings of the National Academy of Sciences of the United States of America · 2018Article
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5 authors.
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Abstract
The Bam complex assembles β-barrel proteins into the outer membrane (OM) of Gram-negative bacteria. These proteins comprise cylindrical β-sheets with long extracellular loops and create pores to allow passage of nutrients and waste products across the membrane. Despite their functional importance, several questions remain about how these proteins are assembled into the OM after their synthesis in the cytoplasm and secretion across the inner membrane. To understand this process better, we studied the assembly of an essential β-barrel substrate for the Bam complex, BamA. By mutating conserved residues in the β-barrel domain of this protein, we generated three assembly-defective BamA substrates that stall early in the folding process in the periplasm. Two of the three defective substrates, which harbor mutations within β-strands, fail to associate productively with the Bam complex. The third substrate, which harbors mutations in a conserved extracellular loop, accumulates on BamD during assembly, but does not integrate efficiently into the membrane. The assembly of all three substrates can be restored by artificially tethering a region of the substrate, which ultimately becomes an extracellular loop, to the lumen of the forming β-barrel. These results imply that a critical step in the folding process involves the interaction of residues on the interior of the nascent β-barrel wall with residues in one of the extracellular loops. We conclude that a prerequisite for membrane integration of β-barrel proteins is burial of the extracellular loops within the forming β-barrel.
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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.