ArticleProceedings of the National Academy of Sciences of the United States of America2023
Driving forces of the complex formation between highly charged disordered proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions.Current opinion in structural biology · 2026Review
- Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.bioRxiv : the preprint server for biology · 2026Article
- A Sequence-Specific Theory for Charge-Regulating IDPs.The journal of physical chemistry. B · 2026Article
- Mapping Charge Interactions in Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Ion NMR for Biomolecular Systems.Journal of molecular biology · 2025Review
- Cooperation and Competition of Base Pairing and Electrostatic Interactions in Mixtures of DNA Nanostars and Polylysine.Journal of the American Chemical Society · 2025Article
- Statistical Physics-Based Approaches to Model the Function and Complexation of Disordered Proteins.The journal of physical chemistry. B · 2025Article
- RNA-peptide interactions tune the ribozyme activity within coacervate microdroplet dispersions.Nature communications · 2025Article
- Progress and Prospects in FRET for the Investigation of Protein-Protein Interactions.Biosensors · 2025Review
- Regulatory role of the N-terminal intrinsically disordered region of the DEAD-box RNA helicase DDX3X in selective RNA recognition.Nature communications · 2025Article
- Competition between Nucleic Acids and Intrinsically Disordered Regions within Proteins.Accounts of chemical research · 2025Article
- Extreme multivalency and a composite short linear motif facilitate PCNA-binding, localisation and abundance of p21 (CDKN1A).The FEBS journal · 2025Article
- Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Article
- Material properties of biomolecular condensates emerge from nanoscale dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The linker histone chaperone Prothymosin α (PTMA) is essential for efficient DNA damage repair and the recruitment of PARP1.Epigenetics & chromatin · 2025Article
- Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025Review
- Role of charges in a dynamic disordered complex between an IDP and a folded domain.Nature communications · 2025Article
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Authors and funding
15 authors.
Funding
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Abstract
Highly disordered complexes between oppositely charged intrinsically disordered proteins present a new paradigm of biomolecular interactions. Here, we investigate the driving forces of such interactions for the example of the highly positively charged linker histone H1 and its highly negatively charged chaperone, prothymosin α (ProTα). Temperature-dependent single-molecule Förster resonance energy transfer (FRET) experiments and isothermal titration calorimetry reveal ProTα-H1 binding to be enthalpically unfavorable, and salt-dependent affinity measurements suggest counterion release entropy to be an important thermodynamic driving force. Using single-molecule FRET, we also identify ternary complexes between ProTα and H1 in addition to the heterodimer at equilibrium and show how they contribute to the thermodynamics observed in ensemble experiments. Finally, we explain the observed thermodynamics quantitatively with a mean-field polyelectrolyte theory that treats counterion release explicitly. ProTα-H1 complex formation resembles the interactions between synthetic polyelectrolytes, and the underlying principles are likely to be of broad relevance for interactions between charged biomolecules in general.
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