ArticleJournal of bacteriology2011
The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Bioinformatics and immunoinformatics assisted multiepitope vaccine construct againstSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024Article
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Construction of a Lectin-Glycan Interaction Network from EnterohemorrhagicInternational journal of molecular sciences · 2020Article
- The small molecule nitazoxanide selectively disrupts BAM-mediated folding of the outer membrane usher protein.The Journal of biological chemistry · 2019Article
- The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.Journal of molecular biology · 2019Article
- Article
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Identifying components required for OMP biogenesis as novel targets for antiinfective drugs.Virulence · 2017Article
- Interfering with outer membrane biogenesis to fight Gram-negative bacterial pathogens.Virulence · 2017Article
- The adaptation ofNPJ microgravity · 2017Article
- Animal Enterotoxigenic Escherichia coli.EcoSal Plus · 2016Review
- Article
- Nitazoxanide Inhibits Pilus Biogenesis by Interfering with Folding of the Usher Protein in the Outer Membrane.Antimicrobial agents and chemotherapy · 2016Article
- Exploitation of a "hockey-puck" phenotype to identify pilus and biofilm regulators in Serratia marcescens through genetic analysis.Canadian journal of microbiology · 2016Article
- A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Secretion systems in Gram-negative bacteria: structural and mechanistic insights.Nature reviews. Microbiology · 2015Review
- Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Microbiology and molecular biology reviews : MMBR · 2014Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fimbrial ushers are the largest β-barrel outer membrane proteins (OMPs) known to date, which function in the polymerization of fimbriae and their translocation to the bacterial surface. Folding and assembly of these complex OMPs are not characterized. Here, we investigate the role of periplasmic chaperones (SurA, Skp, DegP, and FkpA) and individual components of the β-barrel assembly machinery (BAM) complex (BamA, BamB, BamC, and BamE) in the folding of the Escherichia coli FimD usher. The FimD level is dramatically reduced (∼30-fold) in a surA null mutant, but a strong cell envelope stress is constitutively activated with upregulation of DegP (∼10-fold). To demonstrate a direct role of SurA, FimD folding was analyzed in a conditional surA mutant in which SurA expression was controlled. In this strain, FimD is depleted from bacteria in parallel to SurA without significant upregulation of DegP. Interestingly, the dependency on SurA is higher for FimD than for other OMPs. We also demonstrate that a functional BAM complex is needed for folding of FimD. In addition, FimD levels were strongly reduced (∼5-fold) in a mutant lacking the accessory lipoprotein BamB. The critical role of BamB for FimD folding was confirmed by complementation and BamB depletion experiments. Similar to SurA dependency, FimD showed a stronger dependency on BamB than OMPs. On the other hand, folding of FimD was only marginally affected in bamC and bamE mutants. Collectively, our results indicate that FimD usher follows the SurA-BamB pathway for its assembly. The preferential use of this pathway for the folding of OMPs with large β-barrels is discussed.
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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.