ArticleThe Journal of biological chemistry2008
The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE.
Article in The Journal of biological chemistry, 2008. 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.
- Article
- Recruitment of heterologous substrates by bacterial secretion systems for transkingdom translocation.Frontiers in cellular and infection microbiology · 2023Review
- The Ankyrin Repeat Protein RARP-1 Is a Periplasmic Factor That SupportsJournal of bacteriology · 2022Article
- Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021Review
- Identification of a substrate domain that determines system specificity in mycobacterial type VII secretion systems.Scientific reports · 2017Article
- Nuclear Magnetic Resonance Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.Biochemistry · 2015Article
- YscU/FlhB of Yersinia pseudotuberculosis Harbors a C-terminal Type III Secretion Signal.The Journal of biological chemistry · 2015Article
- The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.Journal of molecular biology · 2015Article
- Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein.Biophysical journal · 2014Article
- 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
- A disordered region in the EvpP protein from the type VI secretion system of Edwardsiella tarda is essential for EvpC binding.PloS one · 2014Article
- Intrinsic disorder in pathogen effectors: protein flexibility as an evolutionary hallmark in a molecular arms race.The Plant cell · 2013Article
- A novel C-terminal region within the multicargo type III secretion chaperone CesT contributes to effector secretion.Journal of bacteriology · 2013Article
- The Salmonella type III secretion system inner rod protein PrgJ is partially folded.The Journal of biological chemistry · 2012Article
- 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
- Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARP.Molecular microbiology · 2011Article
- The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.The Journal of biological chemistry · 2011Article
- Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.PloS one · 2011Article
- A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.Molecular bioSystems · 2010Article
- Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus.Molecular microbiology · 2010Article
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4 authors.
Funding
Abstract
Many virulence-related, bacterial effector proteins are translocated directly into the cytosol of host cells by the type III secretion (TTS) system. Translocation of most TTS effectors requires binding by specific chaperones in the bacterial cytosol, although how chaperones promote translocation is unclear. To provide insight into the action of such chaperones, we studied the consequences of binding by the Yersinia chaperone SycE to the effector YopE by NMR. These studies examined the intact form of the effector, whereas prior studies have been limited to well ordered fragments. We found that YopE had the characteristics of a natively unfolded protein, with its N-terminal 100 residues, including its chaperone-binding (Cb) region, flexible and disordered in the absence of SycE. SycE binding caused a pronounced disorder-to-order transition in the Cb region of YopE. The effect of SycE was strictly localized to the Cb region, with other portions of YopE being unperturbed. These results provide stringent limits on models of chaperone action and are consistent with the chaperone promoting formation of a three-dimensional targeting signal in the Cb region of the effector. The target of this putative signal is unknown but appears to be a bacterial component other than the TTS ATPase YscN.
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