Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (129K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Fromant, M.
Right arrow Articles by Blanquet, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fromant, M.
Right arrow Articles by Blanquet, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2003, Vol. 31, No. 12 3227-3235
© 2003 Oxford University Press

Peptidyl-tRNA hydrolase from Sulfolobus solfataricus

Michel Fromant, Maria-Laura Ferri-Fioni, Pierre Plateau and Sylvain Blanquet

Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, 91128 Palaiseau Cedex, France

*To whom correspondence should be addressed. Tel: +33 1 69 33 41 81; Fax: +33 1 69 33 30 13; Email: plateau{at}botrytis.polytechnique.fr

An enzyme capable of liberating functional tRNALys from Escherichia coli diacetyl-lysyl-tRNALys was purified from the archae Sulfolobus solfataricus. Contrasting with the specificity of peptidyl- tRNA hydrolase (PTH) from E.coli, the S.solfataricus enzyme readily accepts E.coli formyl-methionyl-tRNAfMet as a substrate. N-terminal sequencing of this enzyme identifies a gene that has homologs in the whole archaeal kingdom. Involvement of this gene (SS00175) in the recycling of peptidyl-tRNA is supported by its capacity to complement an E.coli strain lacking PTH activity. The archaeal gene, the product of which appears markedly different from bacterial PTHs, also has homologs in all the available eukaryal genomes. Since most of the eukaryotes already display a bacterial-like PTH gene, this observation suggests the occurrence in many eukaryotes of two distinct PTH activities, either of a bacterial or of an archaeal type. Indeed, the bacterial- and archaeal-like genes encoding the two full-length PTHs of Saccharomyces cerevisiae, YHR189w and YBL057c, respectively, can each rescue the growth of an E.coli strain lacking endogeneous PTH. In vitro assays confirm that the two enzymes ensure the recycling of tRNALys from diacetyl-lysyl-tRNALys. Finally, the growth of yeast cells in which either YHR189w or YBL057c has been disrupted was compared under various culture conditions. Evidence is presented that YHR189w, the gene encoding a bacterial-like PTH, should be involved in mitochondrial function.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M.-L. Ferri-Fioni, M. Fromant, A.-P. Bouin, C. Aubard, C. Lazennec, P. Plateau, and S. Blanquet
Identification in Archaea of a Novel D-Tyr-tRNATyr Deacylase
J. Biol. Chem., September 15, 2006; 281(37): 27575 - 27585.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
G. Das and U. Varshney
Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis.
Microbiology, August 1, 2006; 152(Pt 8): 2191 - 2195.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. Soutourina, J. Soutourina, S. Blanquet, and P. Plateau
Formation of D-Tyrosyl-tRNATyr Accounts for the Toxicity of D-Tyrosine toward Escherichia coli
J. Biol. Chem., October 8, 2004; 279(41): 42560 - 42565.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Armengaud, J. Urbonavicius, B. Fernandez, G. Chaussinand, J. M. Bujnicki, and H. Grosjean
N2-Methylation of Guanosine at Position 10 in tRNA Is Catalyzed by a THUMP Domain-containing, S-Adenosylmethionine-dependent Methyltransferase, Conserved in Archaea and Eukaryota
J. Biol. Chem., August 27, 2004; 279(35): 37142 - 37152.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. M. de Pereda, W. F. Waas, Y. Jan, E. Ruoslahti, P. Schimmel, and J. Pascual
Crystal Structure of a Human Peptidyl-tRNA Hydrolase Reveals a New Fold and Suggests Basis for a Bifunctional Activity
J. Biol. Chem., February 27, 2004; 279(9): 8111 - 8115.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.