ArticleThe Journal of biological chemistry2008
Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- High Molecular Weight Protein-Like Semiflexible Chains via Bioorthogonal Polymerization of Coiled-Coil Peptides.Macromolecules · 2024Article
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- Probing Protein Folding with Sequence-Reversed α-Helical Bundles.International journal of molecular sciences · 2021Article
- The Contribution of the Predicted Sorting Platform Component HrcQ to Type III Secretion inFrontiers in microbiology · 2021Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure-function continuum with intrinsic disorder-based proteoforms.Cellular and molecular life sciences : CMLS · 2019Review
- On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome.MedChemComm · 2019Review
- Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes.International journal of molecular sciences · 2017Article
- Probing the average local structure of biomolecules using small-angle scattering and scaling laws.Biophysical journal · 2014Article
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Phylogenetic analysis of a gene cluster encoding an additional, rhizobial-like type III secretion system that is narrowly distributed among Pseudomonas syringae strains.BMC microbiology · 2012Article
- The type III secretion system is necessary for the development of a pathogenic and endophytic interaction between Herbaspirillum rubrisubalbicans and Poaceae.BMC microbiology · 2012Article
- Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway.Biochemistry · 2011Article
- Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins.Cell · 2010Article
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7 authors.
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Abstract
Gene clusters encoding various type III secretion system (T3SS) injectisomes, frequently code downstream of the conserved atpase gene for small hydrophilic proteins whose amino acid sequences display a propensity for intrinsic disorder and coiled-coil formation. These properties were confirmed experimentally for a member of this class, the HrpO protein from the T3SS of Pseudomonas syringae pv phaseolicola: HrpO exhibits high alpha-helical content with coiled-coil characteristics, strikingly low melting temperature, structural properties that are typical for disordered proteins, and a pronounced self-association propensity, most likely via coiled-coil interactions, resulting in heterogeneous populations of quaternary complexes. HrpO interacts in vivo with HrpE, a T3SS protein for which coiled-coil formation is also strongly predicted. Evidence from HrpO analogues from all T3SS families and the flagellum suggests that the extreme flexibility and propensity for coiled-coil interactions of this diverse class of small, intrinsically disordered proteins, whose structures may alter as they bind to their cognate folded protein targets, might be important elements in the establishment of protein-protein interaction networks required for T3SS function.
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