Abstract
The structure of the yeast L-A virus was determined by X-ray crystallography at 3.4 Å resolution. The L-A dsRNA virus is 400 Å in diameter and contains a single protein shell of 60 asymmetric dimers of the coat protein, a feature common among the inner protein shells of dsRNA viruses and probably related to their unique mode of transcription and replication. The two identical subunits in each dimer are in non-equivalent environments and show substantially different conformations in specific surface regions. The L-A virus decaps cellular mRNA to efficiently translate its own uncapped mRNA. Our structure reveals a trench at the active site of the decapping reaction and suggests a role for nearby residues in the reaction.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
Accession codes
References
Wickner, R.B. in Fields Virology 4th edn (eds Knipe, D.M. & Howley, P.M.) 629–658 (Lippincott, Philadelphia; 2001).
Caston, J.R. et al. J. Cell. Biol. 138, 975–985 (1997).
Ribas, J.C. & Wickner, R.B. J. Biol. Chem. 273, 9306–9311 (1998).
Fujimura, T., Ribas, J.C., Makhov, A.M. & Wickner, R.B. Nature 359, 746–749 (1992).
Muhlrad, D., Decker, C.J. & Parker, R. Mol. Cell. Biol. 15, 2145–2156 (1995).
Blanc, A., Goyer, C. & Sonenberg, N. Mol. Cell. Biol. 12, 3390–3398 (1992).
Masison, D.C. et al. Mol. Cell. Biol. 15, 2763–2771 (1995).
Grimes, J.M. et al. Nature 395, 470–478 (1998).
Reinisch, K.M., Nibert, M.L. & Harrison, S.C. Nature 404, 960–967 (2000).
Blanc, A., Ribas, J.C., Wickner, R.B. & Sonenberg, N. Mol. Cell. Biol. 14, 2664–2674 (1994).
Hakansson, K., Doherty, A.J., Shuman, S. & Wigley, D.B. Cell 89, 545–553 (1997).
Gouet, P. et al. Cell 97, 481–490 (1999).
Holm, L. & Sander, C. Science 273, 595–603 (1996).
Koonin, E.V. Semin. Virol. 3, 327–339 (1992).
Fujimura, T., Esteban, R. & Wickner, R.B. Proc. Natl. Acad. Sci. USA 83, 4433–4437 (1986).
Uptain, S.M., Kane, C.M. & Chamberlin, M.J. Annu. Rev. Biochem 66, 117–172 (1997).
Lundquist, R.E., Ehrenfeld, E. & Maizel, J.V. Jr Proc. Natl. Acad. Sci. USA 71, 4773–4477 (1974).
Zarbl, H. & Millward, S. in The Reoviridae (ed. Joklik, W.K.) 107–196 (Plenum; Dordrecht; 1983).
Naitow, H., Canady, M.A., Lin, T., Wickner, R.B. & Johnson, J.E. J. Struct. Biol. 135, 1–7 (2001).
Icho, T. & Wickner, R.B. J. Biol. Chem. 264, 6716–6723 (1989).
Diamond, M.E. et al. J. Virol. 63, 3983–3990 (1989).
Otwinowski, Z. & Minor, W. Methods Enzymol. 277, 505–524 (1997).
Tong, L. & Rossmann, M.G. Methods Enzymol. 276, 594–611 (1997).
Kleywegt, G.J. & Read, R.J. Structure 5, 1557–1569 (1997).
Collaborative Computational Project, Number 4 Acta Crystallogr. D 50, 760–763 (1994).
Read, R.J. Acta Crystallogr. A 42, 140–149 (1986).
Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Acta Crystallogr. A 47, 110–119 (1991).
Brünger, A.T. X-PLOR, version 3.1. (Yale University Press, New Haven; 1992).
Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. J. Appl. Crystallogr. 26, 283–291 (1993).
Sayle, R.A. & Milner-White, E.J. Trends Biochem. Sci. 20, 374 (1995).
Kraulis, P.J. J. Appl. Crystallogr. 24, 946–950 (1991).
Acknowledgements
We thank T. Lin and G. Cingolani for their help in the data collection. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science. Use of the BioCARS Sector 14 was supported by the National Institutes of Health, National Center for Research Resources. The crystallographic studies were supported by a grant from the National Institutes of Health to J.E.J.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing financial interests.
Rights and permissions
About this article
Cite this article
Naitow, H., Tang, J., Canady, M. et al. L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism. Nat Struct Mol Biol 9, 725–728 (2002). https://doi.org/10.1038/nsb844
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/nsb844
This article is cited by
-
Structure and assembly of scalable porous protein cages
Nature Communications (2017)
-
The infectious particle of insect-borne totivirus-like Omono River virus has raised ridges and lacks fibre complexes
Scientific Reports (2016)
-
Characterization of virus-like particles and identification of capsid proteins in Xanthophyllomyces dendrorhous
Virus Genes (2015)
-
Conventional and unconventional mechanisms for capping viral mRNA
Nature Reviews Microbiology (2012)
-
Taming of the shrewd: novel eukaryotic genes from RNA viruses
BMC Biology (2010)