Hidden long evolutionary memory in a model biochemical network.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29758653.
- Also identified by DOI 10.1103/PhysRevE.97.040401 and PMC identifier 5973509.
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Abstract
We introduce a minimal model for the evolution of functional protein-interaction networks using a sequence-based mutational algorithm, and apply the model to study neutral drift in networks that yield oscillatory dynamics. Starting with a functional core module, random evolutionary drift increases network complexity even in the absence of specific selective pressures. Surprisingly, we uncover a hidden order in sequence space that gives rise to long-term evolutionary memory, implying strong constraints on network evolution due to the topology of accessible sequence space.
Medical subject headings
- Evolution, Molecular
- Models, Biological
- Protein Interaction Maps