Barends S, Rudinger-Thirion J, Florentz C, Giege R, Pleij C W, Kraal B
tRNA-like structure regulates translation of Brome mosaic virus RNA Article de journal
Dans: J Virol, vol. 78, no. 8, p. 4003-4010, 2004, ISBN: 15047816, (0022-538x Journal Article).
Résumé | Liens | BibTeX | Étiquettes: ase Sequence Bromovirus/*genetics/metabolism Genetic Complementation Test Genome, FLORENTZ, FRUGIER, Genetic Triticum/virology Tyrosine/chemistry Tyrosine-tRNA Ligase/chemistry/genetics/metabolism Viral Proteins/chemistry/genetics, Non-U.S. Gov't Translation, Transfer/chemistry/genetics RNA, Unité ARN, Viral Molecular Sequence Data Nucleic Acid Conformation RNA, Viral/*chemistry/*genetics Support
@article{,
title = {tRNA-like structure regulates translation of Brome mosaic virus RNA},
author = {S Barends and J Rudinger-Thirion and C Florentz and R Giege and C W Pleij and B Kraal},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15047816},
isbn = {15047816},
year = {2004},
date = {2004-01-01},
journal = {J Virol},
volume = {78},
number = {8},
pages = {4003-4010},
abstract = {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 TLS(TYMV) 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' TLS(BMV) (about 200 nucleotides) with determinants for tyrosylation. We discovered TLS(BMV)-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 TLS(BMV) 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 TLS(BMV) in trans. Intriguingly, a subdomain of the TLS(BMV) could even almost fully restore translation to the original pattern. We discuss here a model with a central and dominant role for the TLS(BMV) during the BMV infection cycle.},
note = {0022-538x
Journal Article},
keywords = {ase Sequence Bromovirus/*genetics/metabolism Genetic Complementation Test Genome, FLORENTZ, FRUGIER, Genetic Triticum/virology Tyrosine/chemistry Tyrosine-tRNA Ligase/chemistry/genetics/metabolism Viral Proteins/chemistry/genetics, Non-U.S. Gov't Translation, Transfer/chemistry/genetics RNA, Unité ARN, Viral Molecular Sequence Data Nucleic Acid Conformation RNA, Viral/*chemistry/*genetics Support},
pubstate = {published},
tppubtype = {article}
}