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deep evolutionary conservation of an intramolecular protein kinase activation mechanism深进化保护分子内的蛋白激酶激活机制.pdf

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deep evolutionary conservation of an intramolecular protein kinase activation mechanism深进化保护分子内的蛋白激酶激活机制

Deep Evolutionary Conservation of an Intramolecular Protein Kinase Activation Mechanism 1. 2. 1 3 4 Jingfen Han , Diego Miranda-Saavedra , Nathan Luebbering , Aman Singh , Gary Sibbet , Michael A. J. 5 1 Ferguson , Vaughn Cleghon * 1 Division of Developmental Biology, Cincinnati Children’s Hospital Medical Center, Cincinnati, Ohio, United States of America, 2 WPI Immunology Frontier Research Center (IFReC) Osaka University, Osaka, Japan, 3 Integrated Program in Biomedical Sciences, University of Tennessee Health Science Center, Memphis, Tennessee, United States of America, 4 Beatson Institute for Cancer Research, Garscube Estate, Glasgow, United Kingdom, 5 Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, United Kingdom Abstract DYRK-family kinases employ an intramolecular mechanism to autophosphorylate a critical tyrosine residue in the activation loop. Once phosphorylated, DYRKs lose tyrosine kinase activity and function as serine/threonine kinases. DYRKs have been characterized in organisms from yeast to human; however, all entities belong to the Unikont supergroup, only one of five eukaryotic supergroups. To assess the evolutionary age and conservation of the DYRK intramolecular kinase-activation mechanism, we surveyed 21 genomes representing four of the five eukaryotic supergroups for the presence of DYRKs. We also analyzed the activation mechanism of the sole DYRK (class 2 DYRK) present in Trypanosoma brucei (TbDYRK2), a member of the excavate supergroup and separated from Drosophila by ,850 million years. Bioinformatics showed the DYRKs clustering into five known subfamili