R. De, L. Tétraboucle-his-'-ggu, . Gcu, . Gca, and . Casnoussi, Gif-sur-Yvette) sur un synthétiseur Amersham Biosciences LKB Gene Assembler, comme décrit précédemment Le rendement final était supérieur à 95%. Pour préparer le duplex His , les oligoribonucléotides 5'-CGC ACU AGC CAG CCC A-3' et 5'-GCU GGC UAG UGC G-3' ont été synthétisés chimiquement comme la tétraboucle His , avec l'aide de Sandrine Caputo (ICSN, Gif-sur-Yvette) Les deux oligonucléotides ont été dialysés contre de l'eau. Leurs concentrations ont été calculées en utilisant des coefficients d'absorbance molaire à 260, pp.155-156, 2001.

. Synthèse-de-la-diacétyl-lyso-'mahony, communication personnelle) : La 3'-amino-3'-désoxyadénosine a été synthétisée comme décrit précédemment (Botta et al., 1998) puis purifiée par une chromatographie sur colonne de gel de silice, éluée avec un mélange méthanol:acétate d'éthyle (12:88, v/v) Ce composé a été obtenu sous forme de poudre incolore avec un rendement global de 5,4 % (pour 10 étapes) La 3'-amino-3'-désoxyadenosine a ensuite été traitée avec du chlorure de tert-butyldiméthylsilyl (TBDMSiCl) (2,2 éq) dans de la pyridine (8 ml) La solution a été évaporée puis purifiée par chromatographie sur une colonne de gel de silice éluée avec un mélange acétate d'éthyle:hexane (7:3, v/v) pour obtenir la 3'-amino-2',5'-bis-O-(tert-butyldiméthyl-silyl)-3'- désoxyadénosine (avec 89% de rendement). La diacétyl-Lys-(3'NH)-adénosine a ensuite été obtenu par un protocole en deux étapes tRNA splicing, Une liaison amide a d'abord été créée entre le composé obtenu précédemment et de la N,N-diacétyl-L-lysine commerciale (Bachem, Suisse) en utilisant, comme agents de couplage, pp.12685-12688, 1998.

I. Ahel, D. Korencic, M. Ibba, and D. Söll, Trans-editing of mischarged tRNAs, Proceedings of the National Academy of Sciences, vol.100, issue.26, pp.15422-15427, 2003.
DOI : 10.1073/pnas.2136934100

I. Ahel, C. Stathopoulos, A. Ambrogelly, A. Sauerwald, H. Toogood et al., Cysteine Activation Is an Inherent in Vitro Property of Prolyl-tRNA Synthetases, Journal of Biological Chemistry, vol.277, issue.38, pp.34743-34748, 2002.
DOI : 10.1074/jbc.M206928200

S. An and K. Musier-forsyth, Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK Protein, Journal of Biological Chemistry, vol.279, issue.41, pp.42359-42362, 2004.
DOI : 10.1074/jbc.C400304200

S. An and K. Musier-forsyth, Cys-tRNAPro Editing by Haemophilus influenzae YbaK via a Novel Synthetase{middle dot}YbaK{middle dot}tRNA Ternary Complex, Journal of Biological Chemistry, vol.280, issue.41, pp.34465-34472, 2005.
DOI : 10.1074/jbc.M507550200

J. G. Arnez, A. C. Dock-bregeon, and D. Moras, Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine, Journal of Molecular Biology, vol.286, issue.5, pp.1449-1459, 1999.
DOI : 10.1006/jmbi.1999.2562

A. G. Atherly and J. R. Menninger, Mutant E. coli Strain with Temperature Sensitive Peptidyltransfer RNA Hydrolase, Nature New Biology, vol.240, issue.103, pp.245-246, 1972.
DOI : 10.1038/newbio240245a0

N. C. Bal, H. Agrawal, A. K. Meher, and A. Arora, Characterization of peptidyl-tRNA hydrolase encoded by open reading frame Rv1014c of Mycobacterium tuberculosis H37Rv, Biological Chemistry, vol.388, issue.5, pp.467-479, 2007.
DOI : 10.1515/BC.2007.057

A. N. Baldwin and P. Berg, Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase, J. Biol. Chem, vol.241, pp.839-845, 1966.

N. Ban, P. Nissen, J. Hansen, P. B. Moore, and T. A. Steitz, The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 A Resolution, Science, vol.289, issue.5481, pp.905-920, 2000.
DOI : 10.1126/science.289.5481.905

K. Beebe, E. Merriman, L. Ribas-de-pouplana, and P. Schimmel, A domain for editing by an archaebacterial tRNA synthetase, Proceedings of the National Academy of Sciences, vol.101, issue.16, pp.5958-5963, 2004.
DOI : 10.1073/pnas.0401530101

K. Beebe, L. Ribas-de-pouplana, and P. Schimmel, Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability, The EMBO Journal, vol.22, issue.3, pp.668-675, 2003.
DOI : 10.1093/emboj/cdg065

R. Benne, N. Naaktgeboren, J. Gubbens, and H. O. Voorma, Recycling of Initiation Factors IF-1, IF-2 and IF-3, European Journal of Biochemistry, vol.277, issue.2, pp.372-380, 1973.
DOI : 10.1016/0006-291X(66)90586-9

P. J. Beuning and K. Musier-forsyth, Hydrolytic editing by a class II aminoacyl-tRNA synthetase, Proceedings of the National Academy of Sciences, vol.97, issue.16, pp.8916-8920, 2000.
DOI : 10.1073/pnas.97.16.8916

P. J. Beuning and K. Musier-forsyth, Species-specific Differences in Amino Acid Editing by Class II Prolyl-tRNA Synthetase, Journal of Biological Chemistry, vol.276, issue.33, pp.30779-30785, 2001.
DOI : 10.1074/jbc.M104761200

S. Blanquet, Y. Mechulam, E. A. Schmitt, and L. Vial, Aminoacyl-Transfer RNA Maturation, Lapointe J. & Brakier- Gringas L., Landes Sciences, pp.65-79, 2003.

O. Botta, E. Moyroud, C. Lobato, and P. Strazewski, Synthesis of 3???-azido- and 3???-amino-3???-deoxyadenosine in both enantiomeric forms, Tetrahedron, vol.54, issue.44, pp.13529-13546, 1998.
DOI : 10.1016/S0040-4020(98)00819-9

F. Bouadloun, D. Donner, and C. G. Kurland, Codon-specific missense errors in vivo, EMBO J, vol.2, pp.1351-1356, 1983.

R. Calendar and P. Berg, d-Tyrosyl RNA: Formation, hydrolysis and utilization for protein synthesis, Journal of Molecular Biology, vol.26, issue.1, pp.39-54, 1967.
DOI : 10.1016/0022-2836(67)90259-8

C. Cerini, P. Kerjan, M. Astier, D. Gratecos, M. Mirande et al., A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase, EMBO J, vol.10, pp.4267-4277, 1991.

G. F. Chen and M. Inouye, genes, Nucleic Acids Research, vol.18, issue.6, pp.1465-1473, 1990.
DOI : 10.1093/nar/18.6.1465
URL : https://hal.archives-ouvertes.fr/hal-01193966

G. T. Chen and M. Inouye, Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli., Genes & Development, vol.8, issue.21, pp.2641-2652, 1994.
DOI : 10.1101/gad.8.21.2641

I. H. Consortium, Finishing the euchromatic sequence of the human genome, International Human Genome Sequencing) Nature, vol.431, pp.931-945, 2004.

K. L. Copeland, J. A. Anderson, A. R. Farley, J. R. Cox, and G. S. Tschumper, Probing Phenylalanine/Adenine ??-Stacking Interactions in Protein Complexes with Explicitly Correlated and CCSD(T) Computations, The Journal of Physical Chemistry B, vol.112, issue.45, pp.14291-14295, 2008.
DOI : 10.1021/jp805528v

T. Crepin, A. Yaremchuk, M. Tukalo, and S. Cusack, Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a cis-Editing Domain, Structure, vol.14, issue.10, pp.1511-1525, 2006.
DOI : 10.1016/j.str.2006.08.007

S. Cusack, Eleven down and nine to go, Nature Structural Biology, vol.2, issue.10, pp.824-831, 1995.
DOI : 10.1107/S0021889891004399

S. Cusack, C. Berthet-colominas, M. Hartlein, N. Nassar, and R. Leberman, A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 ???, Nature, vol.5, issue.6290, pp.249-255, 1990.
DOI : 10.1107/S0021889888009550

S. Cusack, M. Hartlein, and R. Leberman, Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases, Nucleic Acids Research, vol.19, issue.13, pp.3489-3498, 1991.
DOI : 10.1093/nar/19.13.3489

S. Cusack, A. Yaremchuk, and M. Tukalo, The 2 ?? crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue, The EMBO Journal, vol.1080, issue.10, pp.2351-2361, 2000.
DOI : 10.1093/emboj/19.10.2351

F. Cuzin, N. Kretchmer, R. E. Greenberg, R. Hurwitz, and F. Chapeville, Enzymatic hydrolysis of N-substituted aminoacyl-tRNA., Proc. Natl, 1967.
DOI : 10.1073/pnas.58.5.2079

A. Czerwoniec, S. Dunin-horkawicz, E. Purta, K. H. Kaminska, J. M. Kasprzak et al., MODOMICS: a database of RNA modification pathways. 2008 update, Nucleic Acids Research, vol.37, issue.Database, pp.118-121, 2008.
DOI : 10.1093/nar/gkn710
URL : https://hal.archives-ouvertes.fr/hal-00527497

F. Dardel, MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters, Bioinformatics, vol.10, issue.3, pp.273-275, 1994.
DOI : 10.1093/bioinformatics/10.3.273

G. Das and U. Varshney, Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis, Microbiology, vol.152, issue.8, pp.2191-2195, 2006.
DOI : 10.1099/mic.0.29024-0

A. Dock-bregeon, R. Sankaranarayanan, P. Romby, J. Caillet, M. Springer et al., Transfer RNA???Mediated Editing in Threonyl-tRNA Synthetase, Cell, vol.103, issue.6, pp.877-884, 2000.
DOI : 10.1016/S0092-8674(00)00191-4

A. C. Dock-bregeon, B. Rees, A. Torres-larios, G. Bey, J. Caillet et al., Achieving Error-Free Translation, Molecular Cell, vol.16, issue.3, pp.375-386, 2004.
DOI : 10.1016/j.molcel.2004.10.002

M. Domanski, M. Hertzog, J. Coutant, I. Gutsche-perelroizen, F. Bontems et al., Coupling of Folding and Binding of Thymosin ??4 upon Interaction with Monomeric Actin Monitored by Nuclear Magnetic Resonance, Journal of Biological Chemistry, vol.279, issue.22, pp.23637-23645, 2004.
DOI : 10.1074/jbc.M311413200

C. Dominguez, R. Boelens, and A. M. Bonvin, HADDOCK:?? A Protein???Protein Docking Approach Based on Biochemical or Biophysical Information, Journal of the American Chemical Society, vol.125, issue.7, 2003.
DOI : 10.1021/ja026939x

M. Dulic, N. Cvetesic, J. J. Perona, and I. Gruic-sovulj, Partitioning of tRNA-dependent Editing between Pre- and Post-transfer Pathways in Class I Aminoacyl-tRNA Synthetases, Journal of Biological Chemistry, vol.285, issue.31, pp.23799-23809, 2010.
DOI : 10.1074/jbc.M110.133553

S. Dwivedi, S. P. Kruparani, and R. Sankaranarayanan, A D-amino acid editing module coupled to the translational apparatus in archaea, Nature Structural & Molecular Biology, vol.256, issue.6, pp.556-557, 2005.
DOI : 10.1074/jbc.M402931200

M. Edwards, A. Dharamsi, M. Vedadi, M. Domagala, C. Arrowsmith et al., Novel purified polypeptides from Enterococcus faecalis. International application published under the patent cooperation treaty (PCT) WO, 2003.

G. Eriani, J. Cavarelli, F. Martin, L. Ador, B. Rees et al., The class II aminoacyl-tRNA synthetases and their active site: Evolutionary conservation of an ATP binding site, Journal of Molecular Evolution, vol.40, issue.5, pp.499-508, 1995.
DOI : 10.1007/BF00166618

G. Eriani, M. Delarue, O. Poch, J. Gangloff, and D. Moras, Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs, Nature, vol.85, issue.6289, pp.203-206, 1990.
DOI : 10.1016/0022-2836(87)90226-9

D. Evans, S. M. Marquez, and N. R. Pace, RNase P: interface of the RNA and protein worlds, Trends in Biochemical Sciences, vol.31, issue.6, pp.333-341, 2006.
DOI : 10.1016/j.tibs.2006.04.007

S. V. Evans, SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules, Journal of Molecular Graphics, vol.11, issue.2, pp.134-138, 1993.
DOI : 10.1016/0263-7855(93)87009-T

M. L. Ferri-fioni, M. Fromant, A. P. Bouin, C. Aubard, C. Lazennec et al., Identification in Archaea of a Novel D-Tyr-tRNATyr Deacylase, Journal of Biological Chemistry, vol.281, issue.37, pp.27575-27585, 2006.
DOI : 10.1074/jbc.M605860200
URL : https://hal.archives-ouvertes.fr/inserm-00173034

M. L. Ferri-fioni, E. Schmitt, J. Soutourina, P. Plateau, Y. Mechulam et al., Structure of CrystallineD-Tyr-tRNATyr Deacylase: A REPRESENTATIVE OF A NEW CLASS OF tRNA-DEPENDENT HYDROLASES, Journal of Biological Chemistry, vol.276, issue.50, pp.47285-47290, 2001.
DOI : 10.1074/jbc.M106550200

A. R. Fersht, Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase, Biochemistry, vol.16, issue.5, pp.1025-1030, 1977.
DOI : 10.1021/bi00624a034

A. R. Fersht and C. Dingwall, Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions, Biochemistry, vol.18, issue.7, pp.1245-1249, 1979.
DOI : 10.1021/bi00574a020

A. R. Fersht and C. Dingwall, An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis, Biochemistry, vol.18, issue.7, pp.1250-1256, 1979.
DOI : 10.1021/bi00574a021

A. R. Fersht and C. Dingwall, Establishing the misacylation/deacylation of the tRNA pathway for the editing mechanism of prokaryotic and eukaryotic valyl-tRNA synthetases, Biochemistry, vol.18, issue.7, pp.1238-1245, 1979.
DOI : 10.1021/bi00574a019

A. R. Fersht and M. M. Kaethner, Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing, Biochemistry, vol.15, issue.15, pp.3342-3346, 1976.
DOI : 10.1021/bi00660a026

C. Francklyn and P. Schimmel, Enzymatic aminoacylation of an eight-base-pair microhelix with histidine., Proceedings of the National Academy of Sciences, vol.87, issue.21, pp.8655-8659, 1990.
DOI : 10.1073/pnas.87.21.8655

W. Freist, Mechanisms of aminoacyl-tRNA synthetases: a critical consideration of recent results, Biochemistry, vol.28, issue.17, pp.6787-6795, 1989.
DOI : 10.1021/bi00443a001

D. V. Freistroffer, M. Y. Pavlov, J. Macdougall, R. H. Buckingham, and M. Ehrenberg, Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP, 1997.

M. Friedman, -Amino Acids, Journal of Agricultural and Food Chemistry, vol.47, issue.9, 1999.
DOI : 10.1021/jf990080u
URL : https://hal.archives-ouvertes.fr/inria-00357655

L. Frolova, L. Goff, X. Zhouravleva, G. Davydova, E. Philippe et al., Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase, RNA, vol.2, pp.334-341, 1996.

M. Fromant, M. L. Ferri-fioni, P. Plateau, and S. Blanquet, Peptidyl-tRNA hydrolase from Sulfolobus solfataricus, Nucleic Acids Research, vol.31, issue.12, pp.3227-3235, 2003.
DOI : 10.1093/nar/gkg428
URL : https://hal.archives-ouvertes.fr/hal-00770717

M. Fromant, P. Plateau, and S. Blanquet, Function of the Extra 5???-Phosphate Carried by Histidine tRNA, Biochemistry, vol.39, issue.14, pp.4062-4067, 2000.
DOI : 10.1021/bi9923297
URL : https://hal.archives-ouvertes.fr/hal-00771808

M. Fromant, E. Schmitt, Y. Mechulam, C. Lazennec, P. Plateau et al., Peptidyl-tRNA Hydrolase, Biochemistry, vol.44, issue.11, pp.4294-4301, 2005.
DOI : 10.1021/bi047711k
URL : https://hal.archives-ouvertes.fr/hal-00770717

R. Fukunaga and S. Yokoyama, Crystal Structure of Leucyl-tRNA Synthetase from the Archaeon Pyrococcus horikoshii Reveals a Novel Editing Domain Orientation, Journal of Molecular Biology, vol.346, issue.1, pp.57-71, 2005.
DOI : 10.1016/j.jmb.2004.11.060

R. Fukunaga and S. Yokoyama, Structural Basis for Non-cognate Amino Acid Discrimination by the Valyl-tRNA Synthetase Editing Domain, Journal of Biological Chemistry, vol.280, issue.33, pp.29937-29945, 2005.
DOI : 10.1074/jbc.M502668200

R. Fukunaga and S. Yokoyama, Structural Basis for Substrate Recognition by the Editing Domain of Isoleucyl-tRNA Synthetase, Journal of Molecular Biology, vol.359, issue.4, pp.901-912, 2006.
DOI : 10.1016/j.jmb.2006.04.025

M. R. Garcia-villegas, L. De, F. M. Vega, J. M. Galindo, M. Segura et al., Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis, EMBO J, vol.10, pp.3549-3555, 1991.

R. Giegé, Genetic code expansion, Nature Structural Biology, vol.10, issue.6, pp.414-416, 2003.
DOI : 10.1038/nsb0603-414

R. Giegé and M. Frugier, Transfer RNA structure and identity, Landes Sciences, pp.1-24, 2003.

R. Giegé, M. Sissler, and C. Florentz, Universal rules and idiosyncratic features in tRNA identity, Nucleic Acids Research, vol.26, issue.22, pp.5017-5035, 1998.
DOI : 10.1093/nar/26.22.5017

M. Gong, L. R. Cruz-vera, and C. Yanofsky, Ribosome Recycling Factor and Release Factor 3 Action Promotes TnaC-Peptidyl-tRNA Dropoff and Relieves Ribosome Stalling during Tryptophan Induction of tna Operon Expression in Escherichia coli, Journal of Bacteriology, vol.189, issue.8, pp.3147-3155, 2007.
DOI : 10.1128/JB.01868-06

J. J. Goodall, G. J. Chen, and M. G. Page, Peptidyl-tRNA Hydrolase, Biochemistry, vol.43, issue.15, pp.4583-4591, 2004.
DOI : 10.1021/bi0302200

D. S. Goodsell, Inside a living cell, Trends in Biochemical Sciences, vol.16, pp.203-206, 1991.
DOI : 10.1016/0968-0004(91)90083-8

R. Green and H. F. Noller, RIBOSOMES AND TRANSLATION, Annual Review of Biochemistry, vol.66, issue.1, pp.679-716, 1997.
DOI : 10.1146/annurev.biochem.66.1.679

M. Gross, P. Crow, and J. White, The site of hydrolysis by rabbit reticulocyte peptidyl-tRNA hydrolase is the 3'-AMP terminus of susceptible tRNA substrates, J. Biol. Chem, vol.267, pp.2080-2086, 1992.

M. Gross, T. K. Starn, C. Rundquist, P. Crow, J. White et al., Purification and initial characterization of peptidyl-tRNA hydrolase from rabbit reticulocytes, J. Biol. Chem, vol.267, pp.2073-2079, 1992.

I. Gruic-sovulj, N. Uter, T. Bullock, and J. J. Perona, tRNA-dependent Aminoacyl-adenylate Hydrolysis by a Nonediting Class I Aminoacyl-tRNA Synthetase, Journal of Biological Chemistry, vol.280, issue.25, pp.23978-23986, 2005.
DOI : 10.1074/jbc.M414260200

J. M. Guillon, S. Heiss, J. Soutourina, Y. Mechulam, S. Laalami et al., Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli, J. Biol. Chem, vol.271, pp.22321-22325, 1996.

Y. Hagiwara, M. J. Field, O. Nureki, and M. Tateno, Editing Mechanism of Aminoacyl-tRNA Synthetases Operates by a Hybrid Ribozyme/Protein Catalyst, Journal of the American Chemical Society, vol.132, issue.8, 2010.
DOI : 10.1021/ja9095208

R. K. Hartmann, M. Gossringer, B. Spath, S. Fischer, and A. Marchfelder, The making of tRNAs and more -RNase P, 2009.

S. Hati, B. Ziervogel, J. Sternjohn, F. C. Wong, M. C. Nagan et al., Pre-transfer Editing by Class II Prolyl-tRNA Synthetase: ROLE OF AMINOACYLATION ACTIVE SITE IN "SELECTIVE RELEASE" OF NONCOGNATE AMINO ACIDS, Journal of Biological Chemistry, vol.281, issue.38, pp.27862-27872, 2006.
DOI : 10.1074/jbc.M605856200

L. I. Hecht, P. C. Zamecnik, M. L. Stephenson, and J. F. Scott, Nucleoside tri-phosphates as precursors of ribonucleic acid end groups in a mammalian system, J. Biol. Chem, vol.233, pp.954-963, 1958.

T. L. Hendrickson, T. K. Nomanbhoy, V. De-crecy-lagard, S. Fukai, O. Nureki et al., Mutational Separation of Two Pathways for Editing by a Class I tRNA Synthetase, Molecular Cell, vol.9, issue.2, pp.353-362, 2002.
DOI : 10.1016/S1097-2765(02)00449-5

V. Heurgué-hamard, R. Karimi, L. Mora, J. Macdougall, C. Leboeuf et al., Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome, The EMBO Journal, vol.17, issue.3, pp.808-816, 1998.
DOI : 10.1093/emboj/17.3.808

P. H. Hirel, F. Leveque, P. Mellot, F. Dardel, M. Panvert et al., Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase-??-galactosidase chimeric protein, Biochimie, vol.70, issue.6, pp.773-782, 1988.
DOI : 10.1016/0300-9084(88)90107-1

M. B. Hoagland, M. L. Stephenson, J. F. Scott, L. I. Hecht, and P. C. Zamecnik, A soluble ribonucleic acid intermediate in protein synthesis, J. Biol. Chem, vol.231, pp.241-257, 1958.

L. Holm and C. Sander, An evolutionary treasure: unification of a broad set of amidohydrolases related to urease, Proteins: Structure, Function, and Genetics, vol.24, issue.1, pp.72-82, 1997.
DOI : 10.1002/(SICI)1097-0134(199705)28:1<72::AID-PROT7>3.0.CO;2-L

J. J. Hopfield, Kinetic Proofreading: A New Mechanism for Reducing Errors in Biosynthetic Processes Requiring High Specificity, Proceedings of the National Academy of Sciences, vol.71, issue.10, pp.4135-4139, 1974.
DOI : 10.1073/pnas.71.10.4135

C. Hountondji, P. Dessen, and S. Blanquet, Sequence similarities among the family of aminoacyl-tRNA synthetases, Biochimie, vol.68, issue.9, pp.1071-1078, 1986.
DOI : 10.1016/S0300-9084(86)80181-X

T. Hussain, S. P. Kruparani, B. Pal, A. C. Dock-bregeon, S. Dwivedi et al., Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea, The EMBO Journal, vol.266, issue.17, pp.4152-4162, 2006.
DOI : 10.1021/bi012178j
URL : https://hal.archives-ouvertes.fr/hal-00187965

M. Ibba, P. Kast, and H. Hennecke, Substrate Specificity Is Determined by Amino Acid Binding Pocket Size in Escherichia coli Phenylalanyl-tRNA Synthetase, Biochemistry, vol.33, issue.23, pp.7107-7112, 1994.
DOI : 10.1021/bi00189a013

M. Ibba and D. Söll, Quality Control Mechanisms During Translation, Science, vol.286, issue.5446, pp.1893-1897, 1999.
DOI : 10.1126/science.286.5446.1893

M. Ibba and D. Söll, Aminoacyl-tRNA Synthesis, Annual Review of Biochemistry, vol.69, issue.1, pp.617-650, 2000.
DOI : 10.1146/annurev.biochem.69.1.617

H. Jakubowski, Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in the yeast Saccharomyces cerevisiae, EMBO J, vol.10, pp.593-598, 1991.

H. Jakubowski and A. R. Fersht, Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases, Nucleic Acids Research, vol.9, issue.13, pp.3105-3117, 1981.
DOI : 10.1093/nar/9.13.3105

Y. Jan, M. Matter, J. T. Pai, Y. L. Chen, J. Pilch et al., A Mitochondrial Protein, Bit1, Mediates Apoptosis Regulated by Integrins and Groucho/TLE Corepressors, Cell, vol.116, issue.5, pp.751-762, 2004.
DOI : 10.1016/S0092-8674(04)00204-1

B. D. Jenkins and A. Barkan, Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts, The EMBO Journal, vol.20, issue.4, pp.872-879, 2001.
DOI : 10.1093/emboj/20.4.872

R. Kairouz-wahbe, H. Biliran, X. Luo, I. Khor, M. Wankell et al., Anoikis effector Bit1 negatively regulates Erk activity, Proceedings of the National Academy of Sciences, vol.105, issue.5, pp.1528-1532, 2008.
DOI : 10.1073/pnas.0711357105

A. Kaji and G. Hirokawa, Disassembly of post termination complex by RRF (ribosome recycling factor), a possible new target for antimicrobial agents, The Ribosome: Structure, Function, Antibiotics and Cellular Interactions. eds, 2000.

R. Karimi, M. Y. Pavlov, V. Heurgué-hamard, R. H. Buckingham, and M. Ehrenberg, Initiation factors IF1 and IF2 synergistically remove peptidyl-tRNAs with short polypeptides from the P-site of translating Escherichia coli ribosomes, Journal of Molecular Biology, vol.281, issue.2, pp.241-252, 1998.
DOI : 10.1006/jmbi.1998.1953

W. A. Kibbe, OligoCalc: an online oligonucleotide properties calculator, Nucleic Acids Research, vol.35, issue.Web Server, pp.43-46, 2007.
DOI : 10.1093/nar/gkm234

M. Komine, I. M. Freedberg, and M. Blumenberg, Interleukin-1?? Is Released During Transfection of Keratinocytes, Journal of Investigative Dermatology, vol.103, issue.4, pp.580-582, 1994.
DOI : 10.1111/1523-1747.ep12396885

D. Korencic, I. Ahel, J. Schelert, M. Sacher, B. Ruan et al., A freestanding proofreading domain is required for protein synthesis quality control in Archaea, Proceedings of the National Academy of Sciences, vol.101, issue.28, pp.10260-10265, 2004.
DOI : 10.1073/pnas.0403926101

H. Kössel and U. L. Rajbhandary, Studies on polynucleotides, Journal of Molecular Biology, vol.35, issue.3, pp.539-560, 1968.
DOI : 10.1016/S0022-2836(68)80013-0

O. Kotik-kogan, N. Moor, D. Tworowski, and M. Safro, Structural Basis for Discrimination of L-Phenylalanine from L-Tyrosine by Phenylalanyl-tRNA Synthetase, Structure, vol.13, issue.12, pp.1799-1807, 2005.
DOI : 10.1016/j.str.2005.08.013

C. G. Kurland, F. Jørgensen, A. Richter, M. Ehrenberg, N. Bilgin et al., In: The Ribosome ? Structure, Function, and Evolution A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases, Amer. Soc. Microbiol. Biochimie, vol.77, pp.513-526, 1990.

K. Lim, A. Tempczyk, N. Bonander, J. Toedt, A. Howard et al., A Catalytic Mechanism for D-Tyr-tRNATyrDeacylase Based on the Crystal Structure of Hemophilus influenzae HI0670, Journal of Biological Chemistry, vol.278, issue.15, pp.13496-13502, 2003.
DOI : 10.1074/jbc.M213150200

T. L. Lincecum, . Jr, M. Tukalo, A. Yaremchuk, R. S. Mursinna et al., Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase, Molecular Cell, vol.11, issue.4, pp.951-963, 2003.
DOI : 10.1016/S1097-2765(03)00098-4

J. Ling, H. Roy, and M. Ibba, Mechanism of tRNA-dependent editing in translational quality control, Proceedings of the National Academy of Sciences, vol.104, issue.1, pp.72-77, 2007.
DOI : 10.1073/pnas.0606272104

Y. Liu, J. Liao, B. Zhu, E. D. Wang, and J. Ding, leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination, Biochemical Journal, vol.394, issue.2, pp.399-407, 2006.
DOI : 10.1042/BJ20051249

H. F. Lodish and M. Jacobsen, Regulation of hemoglobin synthesis. Equal rates of translation and termination of ?-and ?-globin chains, J. Biol. Chem, vol.247, pp.3622-3629, 1972.

R. B. Loftfield, THE FREQUENCY OF ERRORS IN PROTEIN BIOSYNTHESIS, Biochemical Journal, vol.89, issue.1, pp.82-92, 1963.
DOI : 10.1042/bj0890082

R. B. Loftfield and D. Vanderjagt, The frequency of errors in protein biosynthesis, Biochemical Journal, vol.128, issue.5, pp.1353-1356, 1972.
DOI : 10.1042/bj1281353

S. W. Ludmerer and P. Schimmel, Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases, J. Biol. Chem, vol.262, pp.10801-10806, 1987.

S. Luo and R. L. Levine, Methionine in proteins defends against oxidative stress, The FASEB Journal, vol.23, issue.2, pp.464-472, 2009.
DOI : 10.1096/fj.08-118414

S. A. Martinis and P. Schimmel, Enzymatic aminoacylation of sequencespecific RNA minihelices and hybrid duplexes with methionine, Proc. Natl. Acad, 1992.

J. R. Menninger, Peptidyl transfer RNA dissociates during protein synthesis from ribosomes of Escherichia coli, J. Biol. Chem, vol.251, pp.3392-3398, 1976.

J. R. Menninger, Accumulation of peptidyl tRNA is lethal to Escherichia coli, J. Bacteriol, vol.137, pp.694-696, 1979.

J. F. Milligan and O. C. Uhlenbeck, [5] Synthesis of small RNAs using T7 RNA polymerase, Methods Enzymol, vol.180, pp.51-62, 1989.
DOI : 10.1016/0076-6879(89)80091-6

D. Moras, Structural and functional relationships between aminoacyl-tRNA synthetases, Trends in Biochemical Sciences, vol.17, issue.4, pp.159-164, 1992.
DOI : 10.1016/0968-0004(92)90326-5

K. Musier-forsyth and P. Schimmel, Aminoacylation of RNA oligonucleotides: minimalist structures and origin of specificity, FASEB J, vol.7, pp.282-289, 1993.

N. Netzer, J. M. Goodenbour, A. David, K. A. Dittmar, R. B. Jones et al., Innate immune and chemically triggered oxidative stress modifies translational fidelity, Nature, vol.193, issue.7272, pp.522-526, 2009.
DOI : 10.1038/nature08576

K. J. Newberry, Y. M. Hou, and J. J. Perona, Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase, The EMBO Journal, vol.21, issue.11, pp.2778-2787, 2002.
DOI : 10.1093/emboj/21.11.2778

J. Ninio, Kinetic amplification of enzyme discrimination, Biochimie, vol.57, issue.5, pp.587-595, 1975.
DOI : 10.1016/S0300-9084(75)80139-8

P. Nissen, M. Kjeldgaard, S. Thirup, G. Polekhina, L. Reshetnikova et al., Crystal Structure of the Ternary Complex of Phe-tRNAPhe, EF-Tu, and a GTP Analog, Science, vol.270, issue.5241, pp.1464-1472, 1995.
DOI : 10.1126/science.270.5241.1464

B. E. Nordin and P. Schimmel, Plasticity of Recognition of the 3'-End of Mischarged tRNA by Class I Aminoacyl-tRNA Synthetases, Journal of Biological Chemistry, vol.277, issue.23, pp.20510-20517, 2002.
DOI : 10.1074/jbc.M202023200

K. Nozawa, P. O-'donoghue, S. Gundllapalli, Y. Araiso, R. Ishitani et al., Pyrrolysyl-tRNA synthetase???tRNAPyl structure reveals the molecular basis of orthogonality, Nature, vol.14, issue.7233, pp.1163-1167, 2009.
DOI : 10.1038/nature07611

O. 'mahony, G. Sundgren, A. Svensson, S. Grøtli, and M. , A practical synthesis of 2???-aminoacylamino-2???-deoxyadenosines, Tetrahedron, vol.63, issue.29, pp.6901-6908, 2007.
DOI : 10.1016/j.tet.2007.04.038

J. M. Ogle and V. Ramakrishnan, STRUCTURAL INSIGHTS INTO TRANSLATIONAL FIDELITY, Annual Review of Biochemistry, vol.74, issue.1, pp.129-177, 2005.
DOI : 10.1146/annurev.biochem.74.061903.155440

L. E. Orgel, THE MAINTENANCE OF THE ACCURACY OF PROTEIN SYNTHESIS AND ITS RELEVANCE TO AGEING, Proceedings of the National Academy of Sciences, vol.49, issue.4, pp.517-521, 1963.
DOI : 10.1073/pnas.49.4.517

L. E. Orgel, Ageing of Clones of Mammalian Cells, Nature, vol.234, issue.5408, pp.441-445, 1973.
DOI : 10.1038/243441a0

G. J. Ostheimer, R. Williams-carrier, S. Belcher, E. Osborne, J. Gierke et al., Group II intron splicing factors derived by diversification of an ancient RNA-binding domain, The EMBO Journal, vol.22, issue.15, pp.3919-3929, 2003.
DOI : 10.1093/emboj/cdg372

G. R. Pack, L. Wong, and G. Lamm, PKa of cytosine on the third strand of triplex DNA: Preliminary Poisson-Boltzmann calculations, International Journal of Quantum Chemistry, vol.3, issue.6, pp.1177-1184, 1998.
DOI : 10.1002/(SICI)1097-461X(1998)70:6<1177::AID-QUA7>3.0.CO;2-X

R. D. Palmiter, Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undegraded polysomes and messenger ribonucleic acid, Biochemistry, vol.13, issue.17, pp.3606-3615, 1974.
DOI : 10.1021/bi00714a032

L. Pauling, The probability of errors in the process of synthesis of protein molecules, pp.597-602, 1957.

E. M. Phizicky, Have tRNA, will travel, Proceedings of the National Academy of Sciences, vol.102, issue.32, pp.11127-11128, 2005.
DOI : 10.1073/pnas.0504843102
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1183579

A. V. Pisarev, C. U. Hellen, and T. V. Pestova, Recycling of Eukaryotic Posttermination Ribosomal Complexes, Cell, vol.131, issue.2, pp.286-299, 2007.
DOI : 10.1016/j.cell.2007.08.041

P. Plateau and S. Blanquet, Zinc-dependent synthesis of various dinucleoside 5',5'''-P1,P3-tri- or 5',5'''-P1,P4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase, Biochemistry, vol.21, issue.21, pp.5273-5279, 1982.
DOI : 10.1021/bi00264a024

A. R. Rao and U. Varshney, Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediates peptidyl-tRNA release and ribosome recycling in Escherichia coli, The EMBO Journal, vol.20, issue.11, 2001.
DOI : 10.1093/emboj/20.11.2977

Y. Redko, I. Li-de-lasierra-gallay, and C. Condon, When all's zed and done: the structure and function of RNase Z in prokaryotes, Nature Reviews Microbiology, vol.61, issue.4, pp.278-286, 2007.
DOI : 10.1038/nrmicro1622

N. M. Reynolds, J. Ling, H. Roy, R. Banerjee, S. E. Repasky et al., Cell-specific differences in the requirements for translation quality control, Proceedings of the National Academy of Sciences, vol.107, issue.9, pp.4063-4068, 2010.
DOI : 10.1073/pnas.0909640107

L. Ribas-de-pouplana and P. Schimmel, Aminoacyl-tRNA synthetases: potential markers of genetic code development, Trends in Biochemical Sciences, vol.26, issue.10, pp.591-596, 2001.
DOI : 10.1016/S0968-0004(01)01932-6

F. L. Rock, W. Mao, A. Yaremchuk, M. Tukalo, T. Crepin et al., An Antifungal Agent Inhibits an Aminoacyl-tRNA Synthetase by Trapping tRNA in the Editing Site, Science, vol.316, issue.5832, pp.1759-1761, 2007.
DOI : 10.1126/science.1142189

G. Rosas-sandoval, A. Ambrogelly, J. Rinehart, D. Wei, L. R. Cruz-vera et al., Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast, Proc. Natl. Acad. Sci. U.S.A. 99, pp.16707-16712, 2002.
DOI : 10.1073/pnas.222659199

H. Roy and M. Ibba, Molecular biology: Sticky end in protein synthesis, Nature, vol.56, issue.7107, pp.41-42, 2006.
DOI : 10.1073/pnas.0403926101

H. Roy, J. Ling, J. Alfonzo, and M. Ibba, Loss of Editing Activity during the Evolution of Mitochondrial Phenylalanyl-tRNA Synthetase, Journal of Biological Chemistry, vol.280, issue.46, pp.38186-38192, 2005.
DOI : 10.1074/jbc.M508281200

H. Roy, J. Ling, M. Irnov, and M. Ibba, Post-transfer editing in vitro and in vivo by the ?? subunit of phenylalanyl-tRNA synthetase, The EMBO Journal, vol.92, issue.23, pp.4639-4648, 2004.
DOI : 10.1074/jbc.M309627200

J. Rozenski, P. F. Crain, and J. A. Mccloskey, The RNA Modification Database: 1999 update, Nucleic Acids Research, vol.27, issue.1, pp.196-197, 1999.
DOI : 10.1093/nar/27.1.196

B. Ruan and D. Söll, Deacylase, Journal of Biological Chemistry, vol.280, issue.27, pp.25887-25891, 2005.
DOI : 10.1074/jbc.M502174200

R. Sankaranarayanan, A. C. Dock-bregeon, B. Rees, M. Bovee, J. Caillet et al., Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase, Nat. Struct. Biol, vol.7, pp.461-465, 2000.

R. Sankaranarayanan, A. C. Dock-bregeon, P. Romby, J. Caillet, M. Springer et al., The Structure of Threonyl-tRNA Synthetase-tRNAThr Complex Enlightens Its Repressor Activity and Reveals an Essential Zinc Ion in the Active Site, Cell, vol.97, issue.3, pp.371-381, 1999.
DOI : 10.1016/S0092-8674(00)80746-1

H. M. Sasaki, S. Sekine, T. Sengoku, R. Fukunaga, M. Hattori et al., Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase, Proceedings of the National Academy of Sciences, vol.103, issue.40, pp.14744-14749, 2006.
DOI : 10.1073/pnas.0603182103

A. Sauerwald, W. Zhu, T. A. Major, H. Roy, S. Palioura et al., RNA-Dependent Cysteine Biosynthesis in Archaea, Science, vol.307, issue.5717, pp.1969-1972, 2005.
DOI : 10.1126/science.1108329

E. Schmidt and P. Schimmel, Mutational isolation of a sieve for editing in a transfer RNA synthetase, Science, vol.264, issue.5156, pp.265-267, 1994.
DOI : 10.1126/science.8146659

E. Schmidt and P. Schimmel, Residues in a Class I tRNA Synthetase Which Determine Selectivity of Amino Acid Recognition in the Context of tRNA, Biochemistry, vol.34, issue.35, pp.11204-11210, 1995.
DOI : 10.1021/bi00035a028

E. Schmitt, M. Fromant, P. Plateau, Y. Mechulam, and S. Blanquet, Crystallization and preliminary x???ray analysis of Escherichia coli peptidyl???tRNA hydrolase, Proteins: Structure, Function, and Genetics, vol.28, issue.1, pp.135-136, 1997.
DOI : 10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.3.CO;2-0

E. Schmitt, Y. Mechulam, M. Fromant, P. Plateau, and S. Blanquet, Crystal structure at 1.2Aresolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase, The EMBO Journal, vol.16, issue.15, pp.4760-4769, 1997.
DOI : 10.1093/emboj/16.15.4760
URL : https://hal.archives-ouvertes.fr/hal-00770120

L. H. Schulman and H. Pelka, The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase, J. Biol. Chem, vol.250, pp.542-547, 1975.

M. Selvaraj, S. Roy, N. S. Singh, R. Sangeetha, U. Varshney et al., Structural Plasticity and Enzyme Action: Crystal Structures of Mycobacterium tuberculosis Peptidyl-tRNA Hydrolase, Journal of Molecular Biology, vol.372, issue.1, pp.186-193, 2007.
DOI : 10.1016/j.jmb.2007.06.053

N. Sharma, R. Furter, P. Kast, and D. A. Tirrell, Efficient introduction of aryl bromide functionality into proteins in vivo, FEBS Letters, vol.2, issue.1, pp.37-40, 2000.
DOI : 10.1016/S0014-5793(00)01120-0

A. Sheoran and E. A. First, Activation of D-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase: 2. COOPERATIVE BINDING OF ATP IS LIMITED TO THE INITIAL TURNOVER OF THE ENZYME, Journal of Biological Chemistry, vol.283, issue.19, pp.12971-12980, 2008.
DOI : 10.1074/jbc.M801650200

A. Sheoran, G. Sharma, and E. A. First, Activation of D-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase: 1. PRE-STEADY-STATE KINETIC ANALYSIS REVEALS THE MECHANISTIC BASIS FOR THE RECOGNITION OF D-TYROSINE, Journal of Biological Chemistry, vol.283, issue.19, pp.12960-12970, 2008.
DOI : 10.1074/jbc.M801649200

H. Shi and P. B. Moore, The crystal structure of yeast phenylalanine tRNA at 1.93 ??? resolution: A classic structure revisited, RNA, vol.6, issue.8, pp.1091-1105, 2000.
DOI : 10.1017/S1355838200000364

J. P. Shi, S. A. Martinis, and P. Schimmel, RNA tetraloops as minimalist substrates for aminoacylation, Biochemistry, vol.31, issue.21, pp.4931-4936, 1992.
DOI : 10.1021/bi00136a002

J. Shiloach, S. Bauer, N. De-groot, and Y. Lapidot, The influence of the peptide chain length on the activity of peptidyl-tRNA hydrolase from E. coli, Nucleic Acids Research, vol.2, issue.10, 1941.
DOI : 10.1093/nar/2.10.1941

J. Shiloach, S. Bauer, and Y. Lapidot, Proceedings: Role of the peptide moiety in the interaction between peptidyl-tRNA and peptidyl-tRNA hydrolase, 1975.

K. Shimizu, C. Kuroishi, M. Sugahara, and N. Kunishima, OT3: insight into the functional role of its dimeric state, Acta Crystallographica Section D Biological Crystallography, vol.64, issue.4, pp.444-453, 2008.
DOI : 10.1107/S0907444908002850

S. Shimizu, E. C. Juan, Y. Sato, Y. Miyashita, M. M. Hoque et al., Two Complementary Enzymes for Threonylation of tRNA in Crenarchaeota: Crystal Structure of Aeropyrum pernix Threonyl-tRNA Synthetase Lacking a cis-Editing Domain, Journal of Molecular Biology, vol.394, issue.2, pp.286-296, 2009.
DOI : 10.1016/j.jmb.2009.09.018

A. Sickmann, J. Reinders, Y. Wagner, C. Joppich, R. Zahedi et al., The proteome of Saccharomyces cerevisiae mitochondria, Proceedings of the National Academy of Sciences, vol.100, issue.23, pp.13207-13212, 2003.
DOI : 10.1073/pnas.2135385100

N. S. Singh, R. Ahmad, R. Sangeetha, and U. Varshney, Recycling of Ribosomal Complexes Stalled at the Step of Elongation in Escherichia coli, Journal of Molecular Biology, vol.380, issue.3, pp.451-464, 2008.
DOI : 10.1016/j.jmb.2008.05.033

N. S. Singh and U. Varshney, A physiological connection between tmRNA and peptidyl-tRNA hydrolase functions in Escherichia coli, Nucleic Acids Research, vol.32, issue.20, pp.6028-6037, 2004.
DOI : 10.1093/nar/gkh924

K. Snoussi, S. Nonin-lecomte, and J. L. Leroy, The RNA i-motif, Journal of Molecular Biology, vol.309, issue.1, pp.139-153, 2001.
DOI : 10.1006/jmbi.2001.4618

M. Sokabe, T. Ose, A. Nakamura, K. Tokunaga, O. Nureki et al., The structure of alanyl-tRNA synthetase with editing domain, Proceedings of the National Academy of Sciences, vol.106, issue.27, pp.11028-11033, 2009.
DOI : 10.1073/pnas.0904645106

J. Soutourina, S. Blanquet, and P. Plateau, D-Tyrosyl-tRNATyr Metabolism in Saccharomyces cerevisiae, Journal of Biological Chemistry, vol.275, issue.16, pp.11626-11630, 2000.
DOI : 10.1074/jbc.275.16.11626

J. Soutourina, P. Plateau, and S. Blanquet, Metabolism of D-Aminoacyl-tRNAs inEscherichia coli and Saccharomyces cerevisiae Cells, Journal of Biological Chemistry, vol.275, issue.42, pp.32535-32542, 2000.
DOI : 10.1074/jbc.M005166200

J. Soutourina, P. Plateau, F. Delort, A. Peirotes, and S. Blanquet, Functional characterization of the D-Tyr-tRNA Tyr deacylase from Escherichia coli, J. Biol. Chem, vol.274, 1999.

O. Soutourina, J. Soutourina, S. Blanquet, and P. Plateau, Formation of D-Tyrosyl-tRNATyr Accounts for the Toxicity of D-Tyrosine toward Escherichia coli, Journal of Biological Chemistry, vol.279, issue.41, pp.42560-42565, 2004.
DOI : 10.1074/jbc.M402931200
URL : https://hal.archives-ouvertes.fr/hal-00770709

K. E. Splan, M. E. Ignatov, and K. Musier-forsyth, Transfer RNA Modulates the Editing Mechanism Used by Class II Prolyl-tRNA Synthetase, Journal of Biological Chemistry, vol.283, issue.11, pp.7128-7134, 2008.
DOI : 10.1074/jbc.M709902200

M. Sprinzl, C. Horn, M. Brown, A. Ioudovitch, and S. Steinberg, Compilation of tRNA sequences and sequences of tRNA genes, Nucleic Acids Research, vol.26, issue.1, pp.148-153, 1998.
DOI : 10.1093/nar/26.1.148
URL : https://hal.archives-ouvertes.fr/hal-00356160

G. Srinivasan, C. M. James, and J. A. Krzycki, Pyrrolysine Encoded by UAG in Archaea: Charging of a UAG-Decoding Specialized tRNA, Science, vol.296, issue.5572, pp.1459-1462, 2002.
DOI : 10.1126/science.1069588

L. M. Steinmetz, C. Scharfe, A. M. Deutschbauer, D. Mokranjac, Z. S. Herman et al., Systematic screen for human disease genes in yeast, Nature Genetics, vol.31, pp.400-404, 2002.
DOI : 10.1038/ng929

J. Sternjohn, S. Hati, P. G. Siliciano, and K. Musier-forsyth, Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain, Proceedings of the National Academy of Sciences, vol.104, issue.7, pp.2127-2132, 2007.
DOI : 10.1073/pnas.0611110104

M. A. Swairjo and P. R. Schimmel, Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase, Proc. Natl. Acad, 2005.
DOI : 10.1073/pnas.0409024102

H. Takaku and M. Nashimoto, Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs, Genes Cells, vol.13, pp.1087-1097, 2008.

T. Takarada, Y. Takahata, M. Iemata, E. Hinoi, K. Uno et al., -methyl-D-aspartate receptors composed of NR1 and NR3A subunits in chondrocytes, Journal of Cellular Physiology, vol.63, issue.3, pp.756-764, 2009.
DOI : 10.1016/j.joca.2009.02.002

S. Thanedar, N. V. Kumar, and U. Varshney, The Fate of the Initiator tRNAs Is Sensitive to the Critical Balance between Interacting Proteins, Journal of Biological Chemistry, vol.275, issue.27, pp.20361-20367, 2000.
DOI : 10.1074/jbc.M001238200

A. Torres-larios, K. K. Swinger, T. Pan, and A. Mondragon, Structure of ribonuclease P ??? a universal ribozyme, Current Opinion in Structural Biology, vol.16, issue.3, pp.327-335, 2006.
DOI : 10.1016/j.sbi.2006.04.002

W. C. Tsui and A. R. Fersht, Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli, Nucleic Acids Research, vol.9, issue.18, pp.4627-4637, 1981.
DOI : 10.1093/nar/9.18.4627

G. F. Tu, G. E. Reid, J. G. Zhang, R. L. Moritz, and R. J. Simpson, Cterminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide, J. Biol. Chem, vol.270, pp.9322-9326, 1995.

F. J. Vidales, C. Bernabeu, and J. P. Ballesta, Peptidyl transfer ribonucleic acid hydrolase activity of proteinase K, Biochemistry, vol.18, issue.19, pp.4155-4158, 1979.
DOI : 10.1021/bi00586a016

J. D. Watson and F. H. Crick, Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid, Nature, vol.9, issue.4356, pp.737-738, 1953.
DOI : 10.1016/0006-3002(53)90232-7

A. M. Williams and S. A. Martinis, Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity, Proceedings of the National Academy of Sciences, vol.103, issue.10, pp.3586-3591, 2006.
DOI : 10.1073/pnas.0507362103

B. T. Wimberly, D. E. Brodersen, W. M. Clemons, . Jr, R. J. Morgan-warren et al., Structure of the 30S ribosomal subunit, Nature, vol.407, pp.327-339, 2000.

M. D. Winn, G. N. Murshudov, and M. Z. Papiz, Macromolecular TLS Refinement in REFMAC at Moderate Resolutions, Methods Enzymol, vol.374, pp.300-321, 2003.
DOI : 10.1016/S0076-6879(03)74014-2

D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson et al., 1 H, 13 C and 15 N chemical shift referencing in biomolecular NMR, J. Biomol. NMR, vol.6, pp.135-140, 1995.

D. S. Wishart and B. D. Sykes, The 13 C chemical-shift index: a simple method for the identification of protein secondary structure using 13 C chemicalshift data, J. Biomol. NMR, vol.4, pp.171-180, 1994.

H. Wolosker, S. Blackshaw, and S. H. Snyder, Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission, Proceedings of the National Academy of Sciences, vol.96, issue.23, pp.13409-13414, 1999.
DOI : 10.1073/pnas.96.23.13409

F. C. Wong, P. J. Beuning, C. Silvers, and K. Musier-forsyth, An Isolated Class II Aminoacyl-tRNA Synthetase Insertion Domain Is Functional in Amino Acid Editing, Journal of Biological Chemistry, vol.278, issue.52, pp.52857-52864, 2003.
DOI : 10.1074/jbc.M309627200

K. Wüthrich, NMR of Proteins and Nucleic Acids, 1986.

Y. Xiong and T. A. Steitz, Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template, Nature, vol.31, issue.7000, pp.640-645, 2004.
DOI : 10.1107/S0108767390010224

M. M. Yusupov, G. Z. Yusupova, A. Baucom, K. Lieberman, T. N. Earnest et al., Crystal Structure of the Ribosome at 5.5 A Resolution, Science, vol.292, issue.5518, pp.883-896, 2001.
DOI : 10.1126/science.1060089

H. S. Zaher and R. Green, Fidelity at the Molecular Level: Lessons from Protein Synthesis, Cell, vol.136, issue.4, pp.746-762, 2009.
DOI : 10.1016/j.cell.2009.01.036

H. S. Zaher and R. Green, Quality control by the ribosome following peptide bond formation, Nature, vol.13, issue.7226, pp.161-166, 2009.
DOI : 10.1038/nature07582

H. Zhang, K. Huang, Z. Li, L. Banerjei, K. E. Fisher et al., Crystal structure of YbaK protein fromHaemophilus influenzae (HI1434) at 1.8 ? resolution: Functional implications, Proteins: Structure, Function, and Genetics, vol.10, issue.1, pp.86-97, 2000.
DOI : 10.1002/(SICI)1097-0134(20000701)40:1<86::AID-PROT100>3.0.CO;2-Y

G. Zhouravleva, L. Frolova, L. Goff, X. , L. Guellec et al., Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, pp.1-3, 1995.