ArticleThe Journal of biological chemistry2010
A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Engineering non-pathogenic bacteria for auto-transporter-driven secretion of functional interferon.Gut microbes · 2025Article
- Heterologous Display ofMembranes · 2023Article
- Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms.NPJ biofilms and microbiomes · 2022Article
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Overproducing the BAM complex improves secretion of difficult-to-secrete recombinant autotransporter chimeras.Microbial cell factories · 2021Article
- Recent advances in the understanding of trimeric autotransporter adhesins.Medical microbiology and immunology · 2020Review
- Article
- Inhibition of autotransporter biogenesis by small molecules.Molecular microbiology · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Type V Secretion Systems: An Overview of Passenger Domain Functions.Frontiers in microbiology · 2019Review
- Molecular basis for the folding of β-helical autotransporter passenger domains.Nature communications · 2018Article
- Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.PloS one · 2018Article
- Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a β-Helical Passenger.Frontiers in microbiology · 2017Article
- Secretion of the Intimin Passenger Domain Is Driven by Protein Folding.The Journal of biological chemistry · 2016Article
- Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Molecular microbiology · 2015Review
- The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.The Journal of biological chemistry · 2015Article
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Molecular microbiology · 2015Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp(1015) in the cap region as the most critical residue. Substitution at this position yielded a DegP-sensitive intermediate that is located at the periplasmic side of the OM. Further analysis revealed that Trp(1015) is most likely required for initiation of processive folding of the β-helix at the cell surface, which drives sequential translocation of the Hbp passenger across the OM.
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