ArticleScientific reports2017
Protein interaction evolution from promiscuity to specificity with reduced flexibility in an increasingly complex network.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Stability and interaction defects in the Sin3A-PAH1 αα-hub domain associated with loss-of-function variants.The Journal of biological chemistry · 2026Article
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- Using residue interaction networks to understand protein function and evolution and to engineer new proteins.Current opinion in structural biology · 2024Review
- Key interaction networks: Identifying evolutionarily conserved non-covalent interaction networks across protein families.Protein science : a publication of the Protein Society · 2024Article
- Investigating the Cytotoxicity of Ru(II) Polypyridyl Complexes by Changing the Electronic Structure of Salicylaldehyde Ligands.Inorganic chemistry · 2024Article
- Protein-protein interaction network module changes associated with the vertebrate fin-to-limb transition.Scientific reports · 2023Article
- Transcription factor expression levels and environmental signals constrain transcription factor innovation.Microbiology (Reading, England) · 2023Article
- Cracking the Floral Quartet Code: How Do Multimers of MIKCInternational journal of molecular sciences · 2023Review
- Synergistic Combination ofAntioxidants (Basel, Switzerland) · 2023Article
- Antileukemia Activity and Mechanism of Platinum(II)-Based Metal Complexes.Molecules (Basel, Switzerland) · 2022Article
- Bicalutamide Anticancer Activity Enhancement by Formulation of Soluble Inclusion Complexes with Cyclodextrins.Biomolecules · 2022Article
- αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes.The Journal of biological chemistry · 2022Article
- Stop CRYing! Inhibition of cryptochrome function by small proteins.Biochemical Society transactions · 2022Review
- Genome-Wide Identification and Analysis of the MADS-Box Gene Family in American Beautyberry (Plants (Basel, Switzerland) · 2021Article
- Interaction of selected terpenoids with two SARS-CoV-2 key therapeutic targets: An in silico study through molecular docking and dynamics simulations.Computers in biology and medicine · 2021Article
- On the specificity of protein-protein interactions in the context of disorder.The Biochemical journal · 2021Review
- Were Ancestral Proteins Less Specific?Molecular biology and evolution · 2021Article
- A Fifth of the Protein World: Rossmann-like Proteins as an Evolutionarily Successful Structural unit.Journal of molecular biology · 2021Article
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evolutionary Variation in MADS Box Dimerization Affects Floral Development and Protein Abundance in Maize.The Plant cell · 2020Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key question regarding protein evolution is how proteins adapt to the dynamic environment in which they function and how in turn their evolution shapes the protein interaction network. We used extant and resurrected ancestral plant MADS-domain transcription factors to understand how SEPALLATA3, a protein with hub and glue properties, evolved and takes part in network organization. Although the density of dimeric interactions was saturated in the network, many new interactions became mediated by SEPALLATA3 after a whole genome triplication event. By swapping SEPALLATA3 and its ancestors between dimeric networks of different ages, we found that the protein lost the capacity of promiscuous interaction and acquired specificity in evolution. This was accompanied with constraints on conformations through proline residue accumulation, which made the protein less flexible. SHORT VEGETATIVE PHASE on the other hand (non-hub) was able to gain protein-protein interactions due to a C-terminal domain insertion, allowing for a larger interaction interface. These findings illustrate that protein interaction evolution occurs at the level of conformational dynamics, when the binding mechanism concerns an induced fit or conformational selection. Proteins can evolve towards increased specificity with reduced flexibility when the complexity of the protein interaction network requires specificity.
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