ArticleScience (New York, N.Y.)2018
Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.
Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Evolutionary causes and consequences of gene duplication.Nature reviews. Genetics · 2026Review
- Mass spectrometry reveals the evolutionary conservation of phycobiliprotein complexes.Nature communications · 2026Article
- Phenotypic dominance emerges from activity fitness functions and molecular interactions.Genetics · 2026Article
- Directed evolution of multimeric proteins is enabled by dual-compensatory gene duplication.bioRxiv : the preprint server for biology · 2026Article
- Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape.Nature plants · 2025Article
- Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.bioRxiv : the preprint server for biology · 2024Article
- Pan-Genome-Wide Investigation and Co-Expression Network Analysis ofInternational journal of molecular sciences · 2024Article
- α-Crystalline Domains and Intrinsically Disordered Regions Can Work in Parallel to Induce Accumulation of MBD6 at Chromocenters inEpigenomes · 2024Article
- Mutational biases favor complexity increases in protein interaction networks after gene duplication.Molecular systems biology · 2024Article
- ACD15, ACD21, and SLN regulate the accumulation and mobility of MBD6 to silence genes and transposable elements.Science advances · 2023Article
- Multimeric structure of a subfamily III haloalkane dehalogenase-like enzyme solved by combination of cryo-EM and x-ray crystallography.Protein science : a publication of the Protein Society · 2023Article
- How gene duplication diversifies the landscape of protein oligomeric state and function.Current opinion in genetics & development · 2022Review
- Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.The EMBO journal · 2022Article
- Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities.MedComm · 2022Review
- Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.Chemical science · 2022Article
- Complementing machine learning-based structure predictions with native mass spectrometry.Protein science : a publication of the Protein Society · 2022Article
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Mass Spectrometry-Based Techniques to Elucidate the Sugar Code.Chemical reviews · 2022Review
- Deciphering the molecular organization of GET pathway chaperones through native mass spectrometry.Biophysical journal · 2022Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Oligomeric proteins assemble with exceptional selectivity, even in the presence of closely related proteins, to perform their cellular roles. We show that most proteins related by gene duplication of an oligomeric ancestor have evolved to avoid hetero-oligomerization and that this correlates with their acquisition of distinct functions. We report how coassembly is avoided by two oligomeric small heat-shock protein paralogs. A hierarchy of assembly, involving intermediates that are populated only fleetingly at equilibrium, ensures selective oligomerization. Conformational flexibility at noninterfacial regions in the monomers prevents coassembly, allowing interfaces to remain largely conserved. Homomeric oligomers must overcome the entropic benefit of coassembly and, accordingly, homomeric paralogs comprise fewer subunits than homomers that have no paralogs.
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