Protein interaction evolution from promiscuity to specificity with reduced flexibility in an increasingly complex network.

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 conformati

SUBMITTER: Alhindi T 

PROVIDER: S-EPMC5364480 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature