ArticleNature communications2018
Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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
24 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- T3SS effector and regulator discovery by predicting interacting partners of T3SS chaperones in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2026Article
- Serine phosphorylation of CesT by the type III secretion system effectors NleH1 and NleH2 regulates antagonization of CsrA in enteropathogenicInfection and immunity · 2026Article
- Prokaryotic expression of the giant panda VEGFA gene and the preparation and characterization of its monoclonal antibodies.Veterinary and animal science · 2026Article
- Integrated Transcriptomic and Proteomic Analyses Reveal CsrA-Mediated Regulation of Virulence and Metabolism inMicroorganisms · 2025Article
- The RNA-binding protein ProQ directly binds and regulates virulence genes in enterohemorrhagicFrontiers in cellular and infection microbiology · 2025Article
- T3SS chaperone of the CesT family is required for secretion of the anti-sigma factor BtrA inEmerging microbes & infections · 2023Article
- Spatial Structure Formation by RsmE-Regulated Extracellular Secretions in Pseudomonas fluorescens Pf0-1.Journal of bacteriology · 2022Article
- Article
- Bacterial RNA chaperones and chaperone-like riboregulators: behind the scenes of RNA-mediated regulation of cellular metabolism.RNA biology · 2022Article
- Binding specificity of type three secretion system effector NleH2 to multi-cargo chaperone CesT and their phosphorylation.Protein science : a publication of the Protein Society · 2021Article
- The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches.Frontiers in molecular biosciences · 2021Review
- Small RNA Regulation of Virulence in PathogenicFrontiers in cellular and infection microbiology · 2020Review
- Binding ofFrontiers in microbiology · 2020Article
- Diverse Mechanisms and Circuitry for Global Regulation by the RNA-Binding Protein CsrA.Frontiers in microbiology · 2020Review
- Comparative Genomics and Evolutionary Analysis of RNA-Binding Proteins of the CsrA Family in the GenusFrontiers in molecular biosciences · 2020Article
- Co-Occurrence of theInfection and drug resistance · 2020Article
- Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.Journal of bacteriology · 2019Review
- Article
- Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.Annual review of microbiology · 2019Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The T3SS chaperone CesT is recently shown to interact with the post-transcriptional regulator CsrA to modulate post-attachment signaling in enteropathogenic and enterohemorrhagic Escherichia coli. The molecular basis of the CesT/CsrA binding, however, remains elusive. Here, we show that CesT and CsrA both created two ligand binding sites in their homodimers, forming irregular multimeric complexes in solution. Through construction of a recombinant CsrA-dimer (Re-CsrA) that contains a single CesT binding site, the atomic binding features between CesT and CsrA are delineated via the structure of the CesT/Re-CsrA complex. In contrast to a previously reported N-terminally swapped dimer-form, CesT adopts a dimeric architecture with a swapped C-terminal helix for CsrA engagement. In CsrA, CesT binds to a surface patch that extensively overlaps with its mRNA binding site. The binding mode therefore justifies a mechanism of CsrA-modulation by CesT via competitive inhibition of the CsrA/mRNA interactions.
Identifiers
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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.