ArticleMolecular microbiology2015
Cross-species chimeras reveal BamA POTRA and β-barrel domains must be fine-tuned for efficient OMP insertion.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- The BaeSR two-component system activatesmBio · 2026Article
- 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
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- 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
- Complete genome sequence of Helicobacter pylori B128 7.13 and a single-step method for the generation of unmarked mutations.Helicobacter · 2019Article
- Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.Nature communications · 2018Article
- Article
- Surface display for metabolic engineering of industrially important acetic acid bacteria.PeerJ · 2018Article
- Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori.MicrobiologyOpen · 2017Article
- Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Scientific reports · 2016Article
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
BAM is a conserved molecular machine, the central component of which is BamA. Orthologues of BamA are found in all Gram-negative bacteria, chloroplasts and mitochondria where it is required for the folding and insertion of β-barrel containing integral outer membrane proteins (OMPs) into the outer membrane. BamA binds unfolded β-barrel precursors via the five polypeptide transport-associated (POTRA) domains at its N-terminus. The C-terminus of BamA folds into a β-barrel domain, which tethers BamA to the outer membrane and is involved in OMP insertion. BamA orthologues are found in all Gram-negative bacteria and appear to function in a species-specific manner. Here we investigate the nature of this species-specificity by examining whether chimeric Escherichia coli BamA fusion proteins, carrying either the β-barrel or POTRA domains from various BamA orthologues, can functionally replace E. coli BamA. We demonstrate that the β-barrel domains of many BamA orthologues are functionally interchangeable. We show that defects in the orthologous POTRA domains can be rescued by compensatory mutations within the β-barrel. These data reveal that the POTRA and barrel domains must be precisely aligned to ensure efficient OMP insertion.
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