ArticlePloS one2013
Mutational and topological analysis of the Escherichia coli BamA protein.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Borrelia BBJ25 is a plasmid-encoded Omp85-family protein associated with a potential export system.Bioscience reports · 2026Article
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- Activation of bacterial transcription by distortion of promoter base pairing.Nucleic acids research · 2026Article
- Impact of AbaI mutation on virulence, biofilm development, and antibiotic susceptibility in Acinetobacter baumannii.Scientific reports · 2024Article
- Targeting BamA, the essential component of theHeliyon · 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
- A conserved C-terminal domain of TamB interacts with multiple BamA POTRA domains in Borreliella burgdorferi.PloS one · 2024Article
- Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Inexpensive protein overexpression driven by the NarL transcription activator protein.Biotechnology and bioengineering · 2022Article
- The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) ofFrontiers in molecular biosciences · 2022Article
- BamA and BamD Are Essential for the Secretion of Trimeric Autotransporter Adhesins.Frontiers in microbiology · 2021Article
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- Monoclonal antibody targeting the β-barrel assembly machine ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Escherichia coli "TatExpress" strains super-secrete human growth hormone into the bacterial periplasm by the Tat pathway.Biotechnology and bioengineering · 2017Article
- Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.Biochimica et biophysica acta. Biomembranes · 2017Article
- Regulation of nrf operon expression in pathogenic enteric bacteria: sequence divergence reveals new regulatory complexity.Molecular microbiology · 2017Article
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Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
The multi-protein β-barrel assembly machine (BAM) of Escherichia coli is responsible for the folding and insertion of β-barrel containing integral outer membrane proteins (OMPs) into the bacterial outer membrane. An essential component of this complex is the BamA protein, which binds unfolded β-barrel precursors via the five polypeptide transport-associated (POTRA) domains in its N-terminus. The C-terminus of BamA contains a β-barrel domain, which tethers BamA to the outer membrane and is also thought to be involved in OMP insertion. Here we mutagenize BamA using linker scanning mutagenesis and demonstrate that all five POTRA domains are essential for BamA protein function in our experimental system. Furthermore, we generate a homology based model of the BamA β-barrel and test our model using insertion mutagenesis, deletion analysis and immunofluorescence to identify β-strands, periplasmic turns and extracellular loops. We show that the surface-exposed loops of the BamA β-barrel are essential.
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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.