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 Vitour, D.
Right arrow Articles by Poncet, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vitour, D.
Right arrow Articles by Poncet, D.

 Previous Article  |  Next Article 

Journal of Virology, April 2004, p. 3851-3862, Vol. 78, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.8.3851-3862.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

RoXaN, a Novel Cellular Protein Containing TPR, LD, and Zinc Finger Motifs, Forms a Ternary Complex with Eukaryotic Initiation Factor 4G and Rotavirus NSP3

Damien Vitour, Pierre Lindenbaum,{dagger} Patrice Vende, Michelle M. Becker, and Didier Poncet*

Virologie Moléculaire et Structurale, Unité Mixte de Recherche, CNRS-INRA, 91198 Gif-sur-Yvette, France

Received 22 August 2003/ Accepted 23 December 2003

Rotavirus mRNAs are capped but not polyadenylated, and viral proteins are translated by the cellular translation machinery. This is accomplished through the action of the viral nonstructural protein NSP3, which specifically binds the 3' consensus sequence of viral mRNAs and interacts with the eukaryotic translation initiation factor eIF4G I. To further our understanding of the role of NSP3 in rotavirus replication, we looked for other cellular proteins capable of interacting with this viral protein. Using the yeast two-hybrid assay, we identified a novel cellular protein-binding partner for rotavirus NSP3. This 110-kDa cellular protein, named RoXaN (rotavirus X protein associated with NSP3), contains a minimum of three regions predicted to be involved in protein-protein or nucleic acid-protein interactions. A tetratricopeptide repeat region, a protein-protein interaction domain most often found in multiprotein complexes, is present in the amino-terminal region. In the carboxy terminus, at least five zinc finger motifs are observed, further suggesting the capacity of RoXaN to bind other proteins or nucleic acids. Between these two regions exists a paxillin leucine-aspartate repeat (LD) motif which is involved in protein-protein interactions. RoXaN is capable of interacting with NSP3 in vivo and during rotavirus infection. Domains of interaction were mapped and correspond to the dimerization domain of NSP3 (amino acids 163 to 237) and the LD domain of RoXaN (amino acids 244 to 341). The interaction between NSP3 and RoXaN does not impair the interaction between NSP3 and eIF4G I, and a ternary complex made of NSP3, RoXaN, and eIF4G I can be detected in rotavirus-infected cells, implicating RoXaN in translation regulation.

* Corresponding author. Mailing address: UMR, CNRS-INRA, Virologie Moléculaire et Structurale, 1 avenue de la Terrasse, BÂtiment 14B, 91198 Gif-sur-Yvette Cedex, France. Phone: 33-(0)1 69823835. Fax: 33-(0)1 69824308. E-mail: poncet{at}vms.cnrs-gif.fr.

{dagger} Present address: Integragen, 91000 Evry, France.

Journal of Virology, April 2004, p. 3851-3862, Vol. 78, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.8.3851-3862.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Harb, M., Becker, M. M., Vitour, D., Baron, C. H., Vende, P., Brown, S. C., Bolte, S., Arold, S. T., Poncet, D. (2008). Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN. J. Virol. 82: 11283-11293 [Abstract] [Full Text]  
  • Kimura, T., Kaneko, Y., Yamada, S., Ishihara, H., Senda, T., Iwamatsu, A., Niki, I. (2008). The GDP-dependent Rab27a effector coronin 3 controls endocytosis of secretory membrane in insulin-secreting cell lines. J. Cell Sci. 121: 3092-3098 [Abstract] [Full Text]  
  • Martinez-Salas, E., Pacheco, A., Serrano, P., Fernandez, N. (2008). New insights into internal ribosome entry site elements relevant for viral gene expression. J. Gen. Virol. 89: 611-626 [Abstract] [Full Text]  
  • Tagawa, K., Marubuchi, S., Qi, M.-L., Enokido, Y., Tamura, T., Inagaki, R., Murata, M., Kanazawa, I., Wanker, E. E., Okazawa, H. (2007). The Induction Levels of Heat Shock Protein 70 Differentiate the Vulnerabilities to Mutant Huntingtin among Neuronal Subtypes. J. Neurosci. 27: 868-880 [Abstract] [Full Text]  
  • Perry, C., Sastry, R., Nasrallah, I. M., Stover, P. J. (2005). Mimosine Attenuates Serine Hydroxymethyltransferase Transcription by Chelating Zinc: IMPLICATIONS FOR INHIBITION OF DNA REPLICATION. J. Biol. Chem. 280: 396-400 [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»