ArticleProceedings of the National Academy of Sciences of the United States of America2020
Primordial emergence of a nucleic acid-binding protein via phase separation and statistical ornithine-to-arginine conversion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 101 citations in OpenAlex.
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- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- Protopeptide backbone affects assembly in aqueous solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rapid discovery of new-to-nature protein domains by novelty-first forcing of language models.bioRxiv : the preprint server for biology · 2025Article
- Smart coacervate microdroplets: biomimetic design, material innovations, and emerging applications in biomacromolecule delivery.Bioactive materials · 2025Review
- RNA-peptide interactions tune the ribozyme activity within coacervate microdroplet dispersions.Nature communications · 2025Article
- RNA binding and coacervation promote preservation of peptide form and function across the heterochiral-homochiral divide.Protein science : a publication of the Protein Society · 2025Article
- Coacervate-Based Delivery Systems: Bridging Fundamentals and Applications.ACS applied materials & interfaces · 2025Review
- Functional Ambidexterity of an Ancient Nucleic Acid-Binding Domain.Angewandte Chemie (International ed. in English) · 2025Article
- Biomolecule-Based Coacervation: Mechanisms, Applications, and Future Perspectives in Biomedical and Biotechnological Fields.Biomolecules · 2025Review
- Role of Electron Spin, Chirality, and Charge Dynamics in Promoting the Persistence of Nascent Nucleic Acid-Peptide Complexes.The journal of physical chemistry. B · 2025Article
- From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025Review
- Chemical Evolution of Life on Earth.Genes · 2025Review
- Alternative Pathways in Astrobiology: Reviewing and Synthesizing Contingency and Non-Biomolecular Origins of Terrestrial and Extraterrestrial Life.Life (Basel, Switzerland) · 2024Review
- Peptides En Route from Prebiotic to Biotic Catalysis.Accounts of chemical research · 2024Article
- Sequence, Structure, and Functional Space of Drosophila De Novo Proteins.Genome biology and evolution · 2024Article
- How Droplets Can Accelerate Reactions─Coacervate Protocells as Catalytic Microcompartments.Accounts of chemical research · 2024Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
De novo emergence demands a transition from disordered polypeptides into structured proteins with well-defined functions. However, can polypeptides confer functions of evolutionary relevance, and how might such polypeptides evolve into modern proteins? The earliest proteins present an even greater challenge, as they were likely based on abiotic, spontaneously synthesized amino acids. Here we asked whether a primordial function, such as nucleic acid binding, could emerge with ornithine, a basic amino acid that forms abiotically yet is absent in modern-day proteins. We combined ancestral sequence reconstruction and empiric deconstruction to unravel a gradual evolutionary trajectory leading from a polypeptide to a ubiquitous nucleic acid-binding protein. Intermediates along this trajectory comprise sequence-duplicated functional proteins built from 10 amino acid types, with ornithine as the only basic amino acid. Ornithine side chains were further modified into arginine by an abiotic chemical reaction, improving both structure and function. Along this trajectory, function evolved from phase separation with RNA (coacervates) to avid and specific double-stranded DNA binding. Our results suggest that phase-separating polypeptides may have been an evolutionary resource for the emergence of early proteins, and that ornithine, together with its postsynthesis modification to arginine, could have been the earliest basic amino acids.
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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.