ArticleJournal of bacteriology2010
A solvent-exposed patch in chaperone-bound YopE is required for translocation by the type III secretion system.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Bacterial secretion chaperones: the mycobacterial type VII case.FEMS microbiology letters · 2018Review
- Effector CD8+ T cells are generated in response to an immunodominant epitope in type III effector YopE during primary Yersinia pseudotuberculosis infection.Infection and immunity · 2014Article
- Genetically distinct pathways guide effector export through the type VI secretion system.Molecular microbiology · 2014Article
- Article
- Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion.Cell reports · 2013Article
- A novel C-terminal region within the multicargo type III secretion chaperone CesT contributes to effector secretion.Journal of bacteriology · 2013Article
- A translocator-specific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function.Molecular microbiology · 2012Article
- Expanded roles for multicargo and class 1B effector chaperones in type III secretion.Journal of bacteriology · 2012Review
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion.Biochemistry · 2012Article
- Article
- Translocation of surface-localized effectors in type III secretion.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Most effector proteins of bacterial type III secretion (T3S) systems require chaperone proteins for translocation into host cells. Such effectors are bound by chaperones in a conserved and characteristic manner, with the chaperone-binding (Cb) region of the effector wound around the chaperone in a highly extended conformation. This conformation has been suggested to serve as a translocation signal in promoting the association between the chaperone-effector complex and a bacterial component required for translocation. We sought to test a prediction of this model by identifying a potential association site for the Yersinia pseudotuberculosis chaperone-effector pair SycE-YopE. We identified a set of residues in the YopE Cb region that are required for translocation but are dispensable for expression, SycE binding, secretion into the extrabacterial milieu, and stability in mammalian cells. These residues form a solvent-exposed patch on the surface of the chaperone-bound Cb region, and thus their effect on translocation is consistent with the structure of the chaperone-bound Cb region serving as a signal for translocation.
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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.