The integrated development of network complexity modulates the diverse evolutionary mutation rates of individual proteins.
The rate of evolution-related mutation varies widely among proteins while the unity of the organism implies an integrated evolution of its protein network. Focusing on the yeast interactome, we monitored the structural impact of amino acid substitution on yeast proteins with reported structure. The impact of mutation in creating or deleting structural markers for interactivity varies across proteins and modulates the evolutionary rates, yielding a unified kinetic law of accumulation of connectivities consistent with an integrated evolution of the interactome.
Fernández
Ariel
A
Department of Bioengineering, Rice University, Houston, 77005, USA. arifer@rice.edu
D019943:Amino Acid Substitution / Q000235:genetics; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D011487:Protein Conformation; D025941:Protein Interaction Mapping
D005656:Fungal Proteins