Virus-Encoded Aminoacyl-tRNA Synthetases: Structural and Functional Characterization of Mimivirus TyrRS and MetRS
| Autor: | Jean-Michel Claverie, Joëlle Rudinger-Thirion, Chantal Abergel, Richard Giegé |
|---|---|
| Přispěvatelé: | Information génomique et structurale (IGS), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Architecture et réactivité de l'ARN (ARN), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Martin, Isabelle |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
MESH: Protein Structure
Secondary Acanthamoeba Crystallography X-Ray Protein Structure Secondary chemistry.chemical_compound Tyrosine-tRNA Ligase MESH: Methionine-tRNA Ligase MESH: Acanthamoeba MESH: Animals MESH: Phylogeny Phylogeny Genetics 0303 health sciences 030302 biochemistry & molecular biology Translation (biology) Genetic code MESH: DNA Viruses RNA Transfer Tyr Horizontal gene transfer Transfer RNA RNA Transfer Met Immunology Context (language use) Methionine-tRNA Ligase [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Microbiology Viral Proteins 03 medical and health sciences Eukaryotic translation Virology MESH: Tyrosine-tRNA Ligase Anticodon [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Anticodon MESH: RNA Transfer Tyr Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BC] Life Sciences [q-bio]/Cellular Biology 030304 developmental biology Mimivirus Aminoacyl tRNA synthetase MESH: RNA Transfer Met DNA Viruses biology.organism_classification MESH: Crystallography X-Ray MESH: Viral Proteins Genetic Diversity and Evolution chemistry Insect Science |
| Zdroj: | Journal of Virology Journal of Virology, 2007, pp.12406-12417 Journal of Virology, 2007, 81 (22), pp.12406-17. ⟨10.1128/JVI.01107-07⟩ Journal of Virology, American Society for Microbiology, 2007, 81 (22), pp.12406-17. ⟨10.1128/JVI.01107-07⟩ Journal of Virology, American Society for Microbiology, 2007, pp.12406-12417 Journal of Virology, American Society for Microbiology, 2007, pp.12406-12417. ⟨10.1128⟩ |
| ISSN: | 0022-538X 1098-5514 |
| DOI: | 10.1128/JVI.01107-07⟩ |
| Popis: | Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is translated in amino acids and in providing the substrate for protein synthesis. As such, they fulfill a key role in a process universally conserved in all cellular organisms from their most complex to their most reduced parasitic forms. In contrast, even complex viruses were not found to encode much translation machinery, with the exception of isolated components such as tRNAs. In this context, the discovery of four aminoacyl-tRNA synthetases encoded in the genome of mimivirus together with a full set of translation initiation, elongation, and termination factors appeared to blur what was once a clear frontier between the cellular and viral world. Functional studies of two mimivirus tRNA synthetases confirmed the MetRS specificity for methionine and the TyrRS specificity for tyrosine and conformity with the identity rules for tRNA Tyr for archea/eukarya. The atomic structure of the mimivirus tyrosyl-tRNA synthetase in complex with tyrosinol exhibits the typical fold and active-site organization of archaeal-type TyrRS. However, the viral enzyme presents a unique dimeric conformation and significant differences in its anticodon binding site. The present work suggests that mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas. Their phylogenetic classification does not suggest that they have been acquired recently by horizontal gene transfer from a cellular host but rather militates in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes. |
| Databáze: | OpenAIRE |
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