This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Abergel, C.
Right arrow Articles by Claverie, J.-M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Abergel, C.
Right arrow Articles by Claverie, J.-M.

 Previous Article  |  Next Article 

Journal of Virology, November 2007, p. 12406-12417, Vol. 81, No. 22
0022-538X/07/$08.00+0     doi:10.1128/JVI.01107-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Virus-Encoded Aminoacyl-tRNA Synthetases: Structural and Functional Characterization of Mimivirus TyrRS and MetRS{triangledown}

Chantal Abergel,1* Joëlle Rudinger-Thirion,2 Richard Giegé,2 and Jean-Michel Claverie1

Structural and Genomic Information Laboratory, CNRS-UPR2589, Institut de Biologie Structurale & Microbiologie IFR88, Université de la Méditerranée, 163 avenue de Luminy, Case 934, 13288 Marseille, Cedex 9, France,1 Architecture et Réactivité de l'ARN, CNRS-UPR 9002, IBMC, and Université Louis Pasteur, 15 rue René Descartes, 67084 Strasbourg, France2

Received 22 May 2007/ Accepted 4 September 2007

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 tRNATyr 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.

* Corresponding author. Mailing address: Structural and Genomic Information Laboratory, CNRS-UPR2589, IBSM-IFR88, 163 avenue de Luminy, Case 934, 13288 Marseille, Cedex 9, France. Phone: (33) 491 825422. Fax: (33) 491 825421. E-mail: Chantal.Abergel{at}igs.cnrs-mrs.fr

{triangledown} Published ahead of print on 12 September 2007.

Journal of Virology, November 2007, p. 12406-12417, Vol. 81, No. 22
0022-538X/07/$08.00+0     doi:10.1128/JVI.01107-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jeudy, S., Lartigue, A., Claverie, J.-M., Abergel, C. (2009). Dissecting the Unique Nucleotide Specificity of Mimivirus Nucleoside Diphosphate Kinase. J. Virol. 83: 7142-7150 [Abstract] [Full Text]  
  • Byrne, D., Grzela, R., Lartigue, A., Audic, S., Chenivesse, S., Encinas, S., Claverie, J.-M., Abergel, C. (2009). The polyadenylation site of Mimivirus transcripts obeys a stringent 'hairpin rule'. Genome Res 19: 1233-1242 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»