ArticleProceedings of the National Academy of Sciences of the United States of America2018
Substrate binding to BamD triggers a conformational change in BamA to control membrane insertion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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Who cites it
43 citing papers in PubMed.
- The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Psyllid Cysteine Cathepsins Directly Cleave the Outer Membrane Protein BamD of Citrus Huanglongbing Pathogen.Plant biotechnology journal · 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
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- 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
- Biogenesis of mitochondrial β-barrel membrane proteins.FEBS open bio · 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
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- BamE directly interacts with BamA and BamD coordinating their functions.Molecular microbiology · 2023Article
- Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
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- 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
- Protein domain-dependent vesiculation of Lipoprotein A, a protein that is important in cell wall synthesis and fitness of the human respiratory pathogenFrontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The β-barrel assembly machine (Bam) complex folds and inserts integral membrane proteins into the outer membrane of Gram-negative bacteria. The two essential components of the complex, BamA and BamD, both interact with substrates, but how the two coordinate with each other during assembly is not clear. To elucidate aspects of this process we slowed the assembly of an essential β-barrel substrate of the Bam complex, LptD, by changing a conserved residue near the C terminus. This defective substrate is recruited to the Bam complex via BamD but is unable to integrate into the membrane efficiently. Changes in the extracellular loops of BamA partially restore assembly kinetics, implying that BamA fails to engage this defective substrate. We conclude that substrate binding to BamD activates BamA by regulating extracellular loop interactions for folding and membrane integration.
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