ArticleThe Journal of biological chemistry2016
A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- BamA as a next-generation antibacterial target: mechanistic insights, inhibitor landscape, and rational drug design strategies.RSC advances · 2026Review
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 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
- Monitoring the Interaction of the Peptidoglycan with the Bacterial β-Barrel Assembly Machinery.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Similarly slow diffusion of BAM and SecYEG complexes in live E. coli cells observed with 3D spt-PALM.Biophysical journal · 2023Article
- Surveying membrane landscapes: a new look at the bacterial cell surface.Nature reviews. Microbiology · 2023Review
- Article
- An Unprecedented Tolerance to Deletion of the Periplasmic Chaperones SurA, Skp, and DegP in the Nosocomial Pathogen Acinetobacter baumannii.Journal of bacteriology · 2022Article
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- Article
- Substitutions in SurA and BamA Lead to Reduced Susceptibility to Broad Range Antibiotics in Gonococci.Genes · 2021Article
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.mBio · 2021Article
- The assembly of β-barrel outer membrane proteins.Current opinion in microbiology · 2021Review
- TheInternational journal of molecular sciences · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Pushing the Envelope: The Mysterious Journey Through the Bacterial Secretory Machinery, and Beyond.Frontiers in microbiology · 2021Review
- SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-barrel outer membrane proteins (OMPs) are ubiquitously present in Gram-negative bacteria, mitochondria and chloroplasts, and function in a variety of biological processes. The mechanism by which the hydrophobic nascent β-barrel OMPs are transported through the hydrophilic periplasmic space in bacterial cells remains elusive. Here, mainly via unnatural amino acid-mediated in vivo photo-crosslinking studies, we revealed that the primary periplasmic chaperone SurA interacts with nascent β-barrel OMPs largely via its N-domain but with β-barrel assembly machine protein BamA mainly via its satellite P2 domain, and that the nascent β-barrel OMPs interact with SurA via their N- and C-terminal regions. Additionally, via dual in vivo photo-crosslinking, we demonstrated the formation of a ternary complex involving β-barrel OMP, SurA, and BamA in cells. More importantly, we found that a supercomplex spanning the inner and outer membranes and involving the BamA, BamB, SurA, PpiD, SecY, SecE, and SecA proteins appears to exist in living cells, as revealed by a combined analyses of sucrose-gradient ultra-centrifugation, Blue native PAGE and mass spectrometry. We propose that this supercomplex integrates the translocation, transportation, and membrane insertion events for β-barrel OMP biogenesis.
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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.