Single-cell analysis revealed a strict correspondence between sub-cellular localization of origin domains and their condensation state.
A large-scale in-silico survey that we conducted recently suggests that peptides derived from globular proteins often have the potential to disrupt interactions of their origin domains by competitive inhibition [13], as was previously shown in experiment in several physiological interactions [14], [15].
In summary, protein domains mapped to species trees illustrate evolutionary processes such as the origin of domains, domain loss and transfer, domain combination and divergence.
This implies a consideration of the origin of domains, domain loss, transfer and combination, mapped to the evolutionary history of organisms, specifically the species phylogeny.
By the similar analysis of domain composition of protein, our work also showed that, of the eukaryotic SSU processome proteins, many of the part that arose after the emergence of eukaryotes (i.e., many of those that have no prokaryotic homologs) originated by recruiting archaeal-origin domains, bacterial-origin domains, or both.
Questions relating to the origin of domains, the identification of domain loss, transfer, duplication and combination with other domains to form new proteins, and the formation of the entire protein domain repertoire [2] remain challenging topics in evolutionary biology.
We present a typology of external biophysical stressors, characterizing them in terms of stressor origin, spatial domain and temporal scale.
Such understanding of the evolutionary origin of domains helps to elucidate the functional versatility of known proteins as well as the functionality of hypothetical proteins in human.
