ArticleThe Journal of biological chemistry2014
Membrane and chaperone recognition by the major translocator protein PopB of the type III secretion system of Pseudomonas aeruginosa.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Bordetella BcrH1 and BcrH2 Are Specific Chaperones for the Pore-Forming Complex.Microbiology and immunology · 2026Article
- The sequence of events of enteropathogeniciScience · 2024Article
- Crystallographic Fragment Screening on theACS omega · 2023Article
- Exploring the "N-Terminal Anchor" Binding Interface of the T3SS Chaperone-Translocator Complexes fromBiochemistry · 2023Article
- Recent insights into type-3 secretion system injectisome structure and mechanism of human enteric pathogens.Current opinion in microbiology · 2023Review
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022Review
- Article
- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- AVaccines · 2021Article
- Topological analysis of type 3 secretion translocons in native membranes.Methods in enzymology · 2021Article
- The PopN Gate-keeper Complex Acts on the ATPase PscN to Regulate the T3SS Secretion Switch from Early to Middle Substrates in Pseudomonas aeruginosa.Journal of molecular biology · 2020Article
- Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle ofFrontiers in microbiology · 2019Article
- Visualization of the type III secretion mediatedeLife · 2018Article
- Enhanced differentiation of human pluripotent stem cells into cardiomyocytes by bacteria-mediated transcription factors delivery.PloS one · 2018Article
- Recent advances in understandingF1000Research · 2017Review
- Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.PLoS genetics · 2017Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type III secretion system is a widespread apparatus used by pathogenic bacteria to inject effectors directly into the cytoplasm of eukaryotic cells. A key component of this highly conserved system is the translocon, a pore formed in the host membrane that is essential for toxins to bypass this last physical barrier. In Pseudomonas aeruginosa the translocon is composed of PopB and PopD, both of which before secretion are stabilized within the bacterial cytoplasm by a common chaperone, PcrH. In this work we characterize PopB, the major translocator, in both membrane-associated and PcrH-bound forms. By combining sucrose gradient centrifugation experiments, limited proteolysis, one-dimensional NMR, and β-lactamase reporter assays on eukaryotic cells, we show that PopB is stably inserted into bilayers with its flexible N-terminal domain and C-terminal tail exposed to the outside. In addition, we also report the crystal structure of the complex between PcrH and an N-terminal region of PopB (residues 51-59), which reveals that PopB lies within the concave face of PcrH, employing mostly backbone residues for contact. PcrH is thus the first chaperone whose structure has been solved in complex with both type III secretion systems translocators, revealing that both molecules employ the same surface for binding and excluding the possibility of formation of a ternary complex. The characterization of the major type III secretion system translocon component in both membrane-bound and chaperone-bound forms is a key step for the eventual development of antibacterials that block translocon assembly.
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