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Originally published In Press as doi:10.1074/jbc.M203456200 on June 10, 2002

J. Biol. Chem., Vol. 277, Issue 34, 30445-30453, August 23, 2002
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Lack of Pseudouridine 38/39 in the Anticodon Arm of Yeast Cytoplasmic tRNA Decreases in Vivo Recoding Efficiency*

François LecointeDagger §, Olivier Namy||, Isabelle Hatin, George Simos**Dagger Dagger , Jean-Pierre Rousset, and Henri GrosjeanDagger Dagger Dagger §§

From the Dagger  Laboratoire d'Enzymologie et de Biochimie Structurales, CNRS, 91198 Gif sur Yvette, France,  Institut de Génétique et Microbiologie, Université Paris-Sud, 91405 Orsay, France, and ** Laboratory of Biochemistry, School of Medicine, University of Thessaly, 41222 Larissa, Greece

Many different modified nucleotides are found in naturally occurring tRNA, especially in the anticodon region. Their importance for the efficiency of the translational process begins to be well documented. Here we have analyzed the in vivo effect of deleting genes coding for yeast tRNA-modifying enzymes, namely Pus1p, Pus3p, Pus4p, or Trm4p, on termination readthrough and +1 frameshift events. To this end, we have transformed each of the yeast deletion strains with a lacZ-luc dual-reporter vector harboring selected programmed recoding sites. We have found that only deletion of the PUS3 gene, encoding the enzyme that introduces pseudouridines at position 38 or 39 in tRNA, has an effect on the efficiency of the translation process. In this mutant, we have observed a reduced readthrough efficiency of each stop codon by natural nonsense suppressor tRNAs. This effect is solely due to the absence of pseudouridine 38 or 39 in tRNA because the inactive mutant protein Pus3[D151A]p did not restore the level of natural readthrough. Our results also show that absence of pseudouridine 39 in the slippery tRNA<UP><SUB><IT>UAG</IT></SUB><SUP><IT>Leu</IT></SUP></UP> reduces +1 frameshift efficiency. Therefore, the presence of pseudouridine 38 or 39 in the tRNA anticodon arm enhances misreading of certain codons by natural nonsense tRNAs as well as promotes frameshifting on slippery sequences in yeast.

* This work was supported in part by laboratory funds from the CNRS, Association pour la Recherche sur le Cancer Contract 5297, the Ministère de l'Education Nationale de la Recherche et de la Technologie, from the Association pour la Recherche sur le Cancer Contract 9873 (to H. G.), and Association Française Contre les Myopathies Contract 7757 (to J.-P. R.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Predoctoral fellow supported by a fellowship from the Ministère de la Recherche et de l'Enseignement Supérieur and "Association pour la Recherche sur le Cancer."

|| Predoctoral fellow supported by a fellowship from the Ministère de la Recherche et de l'Enseignement Supérieur. Present address: Dept. of Pathology, Division of Virology, University of Cambridge, Cambridge, UK.

Dagger Dagger Recipient of a grant by the Greek-French Collaboration Program "PLATON."

§§ To whom correspondence should be addressed: CNRS, Laboratoire d'Enzymologie et de Biochimie Structurales, Avenue de la Terrasse, Bat. 34, F-91198 Gif sur Yvette, France. Tel.: 33-1-69-82-34-68; Fax: 33-1-69-82-31-29; E-mail: grosjean@lebs.cnrs-gif.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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