Emergence and evolution of an interaction between intrinsically disordered proteins.

ABSTRACT: Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. However, it is not clear how such interactions emerge and evolve on a molecular level. We performed phylogenetic reconstruction, resurrection and biophysical characterization of two interacting disordered protein domains, CID and NCBD. CID appeared after the divergence of protostomes and deuterostomes 450-600 million years ago, while NCBD was present in the protostome/deuterostome ancestor. The most ancient CID/NCBD formed a relatively weak complex (K_d∼5 µM). At the time of the first vertebrate-specific whole genome duplication, the affinity had increased (K_d∼200 nM) and was maintained in further speciation. Experiment

SUBMITTER: Hultqvist G 

PROVIDER: S-EPMC5419745 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature