A bioinformatic study of septin evolution and co-evolution
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Septins are filamentous GTP-binding proteins that have been found in animals, fungi and microsporidia. This dissertation focuses on a computational study of the septin gene family. The phylogenetic analysis revealed orthologous relationships of septins across kingdoms. It divided all septins into five groups and suggested a consistent nomenclature. Septins interact with themselves as well as other proteins. In protein co-evolution, the interacting proteins change but still maintain protein-protein interactions. A computational method using mutual information was developed to study protein co-evolution and predict protein residue physical interactions for co-evolving positions. This method was applied to the septin gene family to identify co-evolution and interactions among septin subunits, as well as between septins and two proteins, formin and myosin.