common peptides study of aminoacyl-trna synthetases常见的肽研究氨酰合成酶.pdfVIP

Common Peptides Study of Aminoacyl-tRNA Synthetases 1 2 3 4 Assaf Gottlieb *, Milana Frenkel-Morgenstern , Mark Safro , David Horn 1The Balvatnik School of Computer Science, Tel Aviv University, Tel Aviv, Israel, 2 Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre, Madrid, Spain, 3 Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel, 4 School of Physics and Astronomy, Tel Aviv University, Tel Aviv, Israel Abstract Background: Aminoacyl tRNA synthetases (aaRSs) constitute an essential enzyme super-family, providing fidelity of the translation process of mRNA to proteins in living cells. They are common to all kingdoms and are of utmost importance to all organisms. It is thus of great interest to understand the evolutionary relationships among them and underline signature motifs defining their common domains. Results: We utilized the Common Peptides (CPs) framework, based on extracted deterministic motifs from all aaRSs, to study family-specific properties. We identified novel aaRS–class related signatures that may supplement the current classification methods and provide a basis for identifying functional regions specific to each aaRS class. We exploited the space spanned by the CPs in order to identify similarities between aaRS families that are not observed using sequence alignment methods, identifying different inter-aaRS associations across different kingdom of life. We explored the evolutionary history of the aaRS families and evolutionary origins of the mitochondrial aaRSs. Lastly, we showed that prevalent CPs significantly overlap known catalytic and binding sites, suggesting that they have meaningful functional roles, as well as identifying a motif shared between