a novel protein kinase-like domain in a selenoprotein, widespread in the tree of life一种新型蛋白质kinase-like域硒蛋白,广泛在生命之树.pdfVIP

A Novel Protein Kinase-Like Domain in a Selenoprotein, Widespread in the Tree of Life 3 ´ 1 2 1,3 Małgorzata Dudkiewicz , Teresa Szczepinska , Marcin Grynberg , Krzysztof Pawłowski * 1 Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland, 2 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland, 3 Warsaw University of Life Sciences, Warsaw, Poland Abstract Selenoproteins serve important functions in many organisms, usually providing essential oxidoreductase enzymatic activity, often for defense against toxic xenobiotic substances. Most eukaryotic genomes possess a small number of these proteins, usually not more than 20. Selenoproteins belong to various structural classes, often related to oxidoreductase function, yet a few of them are completely uncharacterised. Here, the structural and functional prediction for the uncharacterised selenoprotein O (SELO) is presented. Using bioinformatics tools, we predict that SELO protein adopts a three-dimensional fold similar to protein kinases. Furthermore, we argue that despite the lack of conservation of the ‘‘classic’’ catalytic aspartate residue of the archetypical His-Arg-Asp motif, SELO kinases might have retained catalytic phosphotransferase activity, albeit with an atypical active site. Lastly, the role of the selenocysteine residue is considered and the possibility of an oxidoreductase-regulated kinase function for SELO is discussed. The novel kinase prediction is discussed in the context of functional data on SELO orthologues in model organisms, FMP40 a.k.a.YPL222W (yeast),