TY - JOUR T1 - This Déjà Vu Feeling—Analysis of Multidomain Protein Evolution in Eukaryotic Genomes A1 - Zmasek, Christian M. A1 - Godzik, Adam Y1 - 2012/11/15 N2 - Author Summary Most proteins in eukaryotes are composed of two or more domains, evolutionary independent units with (often) their own individual functions. The specific repertoire of multidomain proteins in a given species defines the topology of pathways and networks that carry out its metabolic and regulatory processes. When proteins with new domain combinations emerge by gene fusion and fission, it directly affects topology of cellular networks in this organism. To better understand the evolution of such networks we analyzed a large set of eukaryotic genomes for the evolutionary history of known domain combinations. Our analysis shows that 70% of all domain combinations present in the human genome independently appeared in at least one other eukaryotic genome. Overall, over 25% of all known multidomain architectures emerged independently several times in the history of life. The difference between a global and species specific picture can be explained by the existence of a core set of domain combinations that keeps reemerging in different species, which are accompanied by a smaller number of unique domain combinations that do not appear anywhere else. JF - PLOS Computational Biology JA - PLOS Computational Biology VL - 8 IS - 11 UR - https://doi.org/10.1371/journal.pcbi.1002701 SP - e1002701 EP - PB - Public Library of Science M3 - doi:10.1371/journal.pcbi.1002701 ER -