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Journal of Virology, April 2004, p. 4003-4010, Vol. 78, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.8.4003-4010.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

tRNA-Like Structure Regulates Translation of Brome Mosaic Virus RNA

Sharief Barends,1,2 Joëlle Rudinger-Thirion,1 Catherine Florentz,1 Richard Giegé,1 Cornelis W. A. Pleij,2 and Barend Kraal2*

UPR 9002 du CNRS, IBMC, F-67084 Strasbourg Cedex, France,1 Department of Biochemistry, Leiden Institute of Chemistry, Leiden University, 2300 RA Leiden, The Netherlands2

Received 27 August 2003/ Accepted 23 December 2003

For various groups of plant viruses, the genomic RNAs end with a tRNA-like structure (TLS) instead of the 3' poly(A) tail of common mRNAs. The actual function of these TLSs has long been enigmatic. Recently, however, it became clear that for turnip yellow mosaic virus, a tymovirus, the valylated TLSTYMV of the single genomic RNA functions as a bait for host ribosomes and directs them to the internal initiation site of translation (with N-terminal valine) of the second open reading frame for the polyprotein. This discovery prompted us to investigate whether the much larger TLSs of a different genus of viruses have a comparable function in translation. Brome mosaic virus (BMV), a bromovirus, has a tripartite RNA genome with a subgenomic RNA4 for coat protein expression. All four RNAs carry a highly conserved and bulky 3' TLSBMV (about 200 nucleotides) with determinants for tyrosylation. We discovered TLSBMV-catalyzed self-tyrosylation of the tyrosyl-tRNA synthetase but could not clearly detect tyrosine incorporation into any virus-encoded protein. We established that BMV proteins do not need TLSBMV tyrosylation for their initiation. However, disruption of the TLSs strongly reduced the translation of genomic RNA1, RNA2, and less strongly, RNA3, whereas coat protein expression from RNA4 remained unaffected. This aberrant translation could be partially restored by providing the TLSBMV in trans. Intriguingly, a subdomain of the TLSBMV could even almost fully restore translation to the original pattern. We discuss here a model with a central and dominant role for the TLSBMV during the BMV infection cycle.

* Corresponding author. Mailing address: Department of Biochemistry, Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, P.O. Box 9502, 2300 RA Leiden, The Netherlands. Phone: (31) 71 527 4770. Fax: (31) 71 527 4340. E-mail: b.kraal{at}chem.leidenuniv.nl.

Journal of Virology, April 2004, p. 4003-4010, Vol. 78, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.8.4003-4010.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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