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

§§
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

*
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.
Present address: Dept. of Pathology, Division of Virology, University of Cambridge, Cambridge, UK.

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.
This article has been cited by other articles:
![]() |
X. Zhao, J. R. Patton, S. K. Ghosh, N. Fischel-Ghodsian, L. Shen, and R. A. Spanjaard Pus3p- and Pus1p-Dependent Pseudouridylation of Steroid Receptor RNA Activator Controls a Functional Switch that Regulates Nuclear Receptor Signaling Mol. Endocrinol., March 1, 2007; 21(3): 686 - 699. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Fernandez-Vizarra, A. Berardinelli, L. Valente, V. Tiranti, and M. Zeviani Nonsense mutation in pseudouridylate synthase 1 (PUS1) in two brothers affected by myopathy, lactic acidosis and sideroblastic anaemia (MLASA) J. Med. Genet., March 1, 2007; 44(3): 173 - 180. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. A. COPELA, G. CHAKSHUSMATHI, R. L. SHERRER, and S. L. WOLIN The La protein functions redundantly with tRNA modification enzymes to ensure tRNA structural stability. RNA, April 1, 2006; 12(4): 644 - 654. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. KWAPISZ, P. CHOLBINSKI, A. K. HOPPER, J.-P. ROUSSET, and T. ZOLADEK Rsp5 ubiquitin ligase modulates translation accuracy in yeast Saccharomyces cerevisiae RNA, November 1, 2005; 11(11): 1710 - 1718. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. F. Agris Decoding the genome: a modified view Nucleic Acids Res., January 9, 2004; 32(1): 223 - 238. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |