Hidden long evolutionary memory in a model biochemical network

Phys Rev E. 2018 Apr;97(4-1):040401. doi: 10.1103/PhysRevE.97.040401.

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.

MeSH terms

  • Evolution, Molecular*
  • Models, Biological*
  • Mutation
  • Protein Interaction Maps*