Two classes of EF1-family translational GTPases encoded by giant viruses
| Autor: | Alexandra Zinoviev, Tatyana V. Pestova, Christopher U.T. Hellen, Kazushige Kuroha |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Marseilleviridae
GTPase GTP Phosphohydrolases 03 medical and health sciences Peptide Elongation Factor 1 Genetics Cluster Analysis Humans Mimiviridae Giant Virus Amoeba Molecular Biology Phylogeny Monomeric GTP-Binding Proteins 030304 developmental biology Acanthamoeba castellanii 0303 health sciences Multiple sequence alignment biology Hydrolysis 030302 biochemistry & molecular biology Marseillevirus Translation (biology) Peptide Chain Termination Translational biology.organism_classification Eukaryotic translation elongation factor 1 alpha 1 Giant Viruses Protein Biosynthesis Guanosine Triphosphate Ribosomes Peptide Termination Factors Protein Binding |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkz296 |
| Popis: | Giant viruses have extraordinarily large dsDNA genomes, and exceptionally, they encode various components of the translation apparatus, including tRNAs, aminoacyl-tRNA synthetases and translation factors. Here, we focused on the elongation factor 1 (EF1) family of viral translational GTPases (trGTPases), using computational and functional approaches to shed light on their functions. Multiple sequence alignment indicated that these trGTPases clustered into two groups epitomized by members of Mimiviridae and Marseilleviridae, respectively. trGTPases in the first group were more closely related to GTP-binding protein 1 (GTPBP1), whereas trGTPases in the second group were closer to eEF1A, eRF3 and Hbs1. Functional characterization of representative GTPBP1-like trGTPases (encoded by Hirudovirus, Catovirus and Moumouvirus) using in vitro reconstitution revealed that they possess eEF1A-like activity and can deliver cognate aa-tRNAs to the ribosomal A site during translation elongation. By contrast, representative eEF1A/eRF3/Hbs1-like viral trGTPases, encoded by Marseillevirus and Lausannevirus, have eRF3-like termination activity and stimulate peptide release by eRF1. Our analysis identified specific aspects of the functioning of these viral trGTPases with eRF1 of human, amoebal and Marseillevirus origin. |
| Databáze: | OpenAIRE |
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