ArticleProceedings of the National Academy of Sciences of the United States of America2025
Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Tunable AMPA receptor function via recurrent evolution of heterotetramers.The Journal of general physiology · 2026Article
- Mechanisms of Phenotypic Evolution from Molecules to Organisms: Integrating Evolutionary Biochemistry and Evolutionary Developmental Biology.Annual review of ecology, evolution, and systematics · 2026Article
- Ancestral proteins trace the emergence of substrate specificity and oligomerization within bacterial DEDDy dinucleases.Science advances · 2026Article
- Evolutionary causes and consequences of gene duplication.Nature reviews. Genetics · 2026Review
- Origins of allostery in vertebrate hemoglobin evolution.bioRxiv : the preprint server for biology · 2026Article
- Phenotypic dominance emerges from activity fitness functions and molecular interactions.Genetics · 2026Article
- A functional and applied perspective of Vitreoscilla hemoglobin: from oxygen carriage to biotechnological innovation.Biotechnology letters · 2025Review
- Simple genetic mechanisms toward more intricate molecular complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Abstract
Many proteins form paralogous multimers-molecular complexes in which evolutionarily related proteins are arranged into specific quaternary structures. Little is known about the mechanisms by which they acquired their stoichiometry (the number of total subunits in the complex) and heterospecificity (the preference of subunits for their paralogs rather than other copies of the same protein). Here, we use ancestral protein reconstruction and biochemical experiments to study historical increases in stoichiometry and specificity during the evolution of vertebrate hemoglobin (Hb), an α
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