ArticleInternational journal of molecular sciences2018
Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023Review
- Chasing long-range evolutionary couplings in the AlphaFold era.Biopolymers · 2023Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.Protein science : a publication of the Protein Society · 2022Article
- Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation.Nucleic acids research · 2021Article
- Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.The Journal of biological chemistry · 2020Article
- Evolutionary Study of Disorder in Protein Sequences.Biomolecules · 2020Article
- Macromolecular Interactions of Disordered Proteins.International journal of molecular sciences · 2020Article
- Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins.Biomolecules · 2019Review
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Authors and funding
3 authors.
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Abstract
Although improved strategies for the detection and analysis of evolutionary couplings (ECs) between protein residues already enable the prediction of protein structures and interactions, they are mostly restricted to conserved and well-folded proteins. Whereas intrinsically disordered proteins (IDPs) are central to cellular interaction networks, due to the lack of strict structural constraints, they undergo faster evolutionary changes than folded domains. This makes the reliable identification and alignment of IDP homologs difficult, which led to IDPs being omitted in most large-scale residue co-variation analyses. By preforming a dedicated analysis of phylogenetically widespread bacterial IDP⁻partner interactions, here we demonstrate that partner binding imposes constraints on IDP sequences that manifest in detectable interprotein ECs. These ECs were not detected for interactions mediated by short motifs, rather for those with larger IDP⁻partner interfaces. Most identified coupled residue pairs reside close (<10 Å) to each other on the interface, with a third of them forming multiple direct atomic contacts. EC-carrying interfaces of IDPs are enriched in negatively charged residues, and the EC residues of both IDPs and partners preferentially reside in helices. Our analysis brings hope that IDP⁻partner interactions difficult to study could soon be successfully dissected through residue co-variation analysis.
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