ArticleProceedings of the National Academy of Sciences of the United States of America2011
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
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- Redefining the Limits of Functional Continuity in the Early Evolution of P-Loop NTPases.Molecular biology and evolution · 2025Article
- From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025Review
- Ancestral Reconstruction and the Evolution of Protein Energy Landscapes.Annual review of biophysics · 2024Review
- Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins.Nature chemistry · 2024Article
- Primitive purine biosynthesis connects ancient geochemistry to modern metabolism.Nature ecology & evolution · 2024Article
- Back in time to the Gly-rich prototype of the phosphate binding elementary function.Current research in structural biology · 2024Review
- Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.Frontiers in molecular biosciences · 2023Article
- Why we are made of proteins and nucleic acids: Structural biology views on extraterrestrial life.Biophysics and physicobiology · 2023Article
- Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022Article
- Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022Review
- Functionalization of a symmetric protein scaffold: Redundant folding nuclei and alternative oligomeric folding pathways.Protein science : a publication of the Protein Society · 2022Article
- Gene Fusion and Directed Evolution to Break Structural Symmetry and Boost Catalysis by an Oligomeric C-C Bond-Forming Enzyme.Angewandte Chemie (International ed. in English) · 2022Article
- Evidence for the emergence of β-trefoils by 'Peptide Budding' from an IgG-like β-sandwich.PLoS computational biology · 2022Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- The ubiquitous buried water in the beta-trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy.Protein science : a publication of the Protein Society · 2021Article
- Topological and Structural Plasticity of the Single Ig Fold and the Double Ig Fold Present in CD19.Biomolecules · 2021Article
- Evolution of a σ-(c-di-GMP)-anti-σ switch.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cooperative hydrophobic core interactions in the β-trefoil architecture.Protein science : a publication of the Protein Society · 2021Article
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The majority of protein architectures exhibit elements of structural symmetry, and "gene duplication and fusion" is the evolutionary mechanism generally hypothesized to be responsible for their emergence from simple peptide motifs. Despite the central importance of the gene duplication and fusion hypothesis, experimental support for a plausible evolutionary pathway for a specific protein architecture has yet to be effectively demonstrated. To address this question, a unique "top-down symmetric deconstruction" strategy was utilized to successfully identify a simple peptide motif capable of recapitulating, via gene duplication and fusion processes, a symmetric protein architecture (the threefold symmetric β-trefoil fold). The folding properties of intermediary forms in this deconstruction agree precisely with a previously proposed "conserved architecture" model for symmetric protein evolution. Furthermore, a route through foldable sequence-space between the simple peptide motif and extant protein fold is demonstrated. These results provide compelling experimental support for a plausible evolutionary pathway of symmetric protein architecture via gene duplication and fusion processes.
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