ArticleJournal of molecular biology2015
In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 71 citations in OpenAlex.
- BamA as a next-generation antibacterial target: mechanistic insights, inhibitor landscape, and rational drug design strategies.RSC advances · 2026Review
- 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
- Article
- Effects of pleiotropicJournal of bacteriology · 2024Article
- Attenuated vaccine PmCQ2Δ4555-4580 effectively protects mice against Pasteurella multocida infection.BMC veterinary research · 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
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- Transcriptomic analysis approach towards an improved tolerance of Escherichia coli to gallic acid stress.Archives of microbiology · 2023Article
- Assembly mechanism of a Tad secretion system secretin-pilotin complex.Nature communications · 2023Article
- BamE directly interacts with BamA and BamD coordinating their functions.Molecular microbiology · 2023Article
- High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mode of action of lipoprotein modification enzymes-Novel antibacterial targets.Molecular microbiology · 2021Review
- Bacterial Lipoprotein Posttranslational Modifications. New Insights and Opportunities for Antibiotic and Vaccine Development.Frontiers in microbiology · 2021Review
- Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.Journal of bacteriology · 2020Article
- The gain-of-function alleleProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of a Compound That Inhibits the Growth of Gram-Negative Bacteria by Blocking BamA-BamD Interaction.Frontiers in microbiology · 2020Article
- Suppressor Mutations inJournal of bacteriology · 2019Article
- Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate.mBio · 2019Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Assembly of the β-barrel outer membrane proteins (OMPs) is an essential cellular process in Gram-negative bacteria and in the mitochondria and chloroplasts of eukaryotes--two organelles of bacterial origin. Central to this process is the conserved β-barrel OMP that belongs to the Omp85 superfamily. In Escherichia coli, BamA is the core β-barrel OMP and, together with four outer membrane lipoproteins, BamBCDE, constitutes the β-barrel assembly machine (BAM). In this paper, we investigated the roles of BamD, an essential lipoprotein, and BamB in BamA biogenesis. Depletion of BamD caused impairment in BamA biogenesis and cessation of cell growth. These defects of BamD depletion were partly reversed by single-amino-acid substitutions mapping within the β-barrel domain of BamA. However, in the absence of BamB, the positive effects of the β-barrel substitutions on BamA biogenesis under BamD depletion conditions were nullified. By employing a BamA protein bearing one such substitution, F474L, it was demonstrated that the mutant BamA protein could not only assemble without BamD but also facilitate the assembly of wild-type BamA expressed in trans. Based on these data, we propose a model in which the Bam lipoproteins, which are localized to the outer membrane by the BAM-independent Lol pathway, aid in the creation of new BAM complexes by serving as outer membrane receptors and folding factors for nascent BamA molecules. The newly assembled BAM holocomplex then catalyzes the assembly of substrate OMPs and BamA. These in vivo findings are corroborated by recently published in vitro data.
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