ArticleThe Journal of biological chemistry2014
Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 33 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC inmSphere · 2024Article
- The sequence of events of enteropathogeniciScience · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Delineating specific regions of N- terminal domain of T3SS ATPase YsaN ofFrontiers in molecular biosciences · 2022Article
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens.Veterinary research · 2021Review
- The T3SS ofMicroorganisms · 2020Review
- 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
- "The structure of the Type III secretion system export gate with CdsO, an ATPase lever arm".PLoS pathogens · 2020Article
- Dominant negative effects by inactive Spa47 mutants inhibit T3SS function and Shigella virulence.PloS one · 2020Article
- Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.Protein science : a publication of the Protein Society · 2019Article
- On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome.MedChemComm · 2019Review
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
- SrcA is a chaperone for the Salmonella SPI-2 type three secretion system effector SteD.Microbiology (Reading, England) · 2019Article
- Shutting Down Shigella Secretion: Characterizing Small Molecule Type Three Secretion System ATPase Inhibitors.Biochemistry · 2018Article
- Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromFrontiers in microbiology · 2018Article
- Structural and Biochemical Characterization of Spa47 Provides Mechanistic Insight into Type III Secretion System ATPase Activation and Shigella Virulence Regulation.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
A number of Gram-negative pathogens utilize type III secretion systems (T3SSs) to inject bacterial effector proteins into the host. An important component of T3SSs is a conserved ATPase that captures chaperone-effector complexes and energizes their dissociation to facilitate effector translocation. To date, there has been limited work characterizing the chaperone-T3SS ATPase interaction despite it being a fundamental aspect of T3SS function. In this study, we present the 2.1 Å resolution crystal structure of the Salmonella enterica SPI-2-encoded ATPase, SsaN. Our structure revealed a local and functionally important novel feature in helix 10 that we used to define the interaction domain relevant to chaperone binding. We modeled the interaction between the multicargo chaperone, SrcA, and SsaN and validated this model using mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction. Finally, we quantified the benefit of this molecular interaction on bacterial fitness in vivo using chromosomal exchange of wild-type ssaN with mutants that retain ATPase activity but no longer capture the chaperone. Our findings provide insight into chaperone recognition by T3SS ATPases and demonstrate the importance of the chaperone-T3SS ATPase interaction for the pathogenesis of Salmonella.
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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.