C. E. Aitken and J. R. Lorsch, A mechanistic overview of translation initiation in eukaryotes, Nature Structural & Molecular Biology, vol.16, issue.6, pp.568-576, 2012.
DOI : 10.1186/1752-0509-5-131

A. G. Hinnebusch, Molecular Mechanism of Scanning and Start Codon Selection in Eukaryotes, Microbiology and Molecular Biology Reviews, vol.75, issue.3, pp.434-467, 2011.
DOI : 10.1128/MMBR.00008-11

F. L. Erickson and E. M. Hannig, Ligand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunit, EMBO J, vol.15, pp.6311-6320, 1996.

L. D. Kapp and J. R. Lorsch, GTP-dependent Recognition of the Methionine Moiety on Initiator tRNA by Translation Factor eIF2, Journal of Molecular Biology, vol.335, issue.4, pp.923-936, 2004.
DOI : 10.1016/j.jmb.2003.11.025

N. Pedulla, R. Palermo, D. Hasenohrl, U. Blasi, P. Cammarano et al., The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor, Nucleic Acids Research, vol.33, issue.6, pp.1804-1812, 2005.
DOI : 10.1093/nar/gki321

L. Yatime, Y. Mechulam, S. Blanquet, and E. Schmitt, Structural Switch of the ?? Subunit in an Archaeal aIF2???? Heterodimer, Structure, vol.14, issue.1, pp.119-128, 2006.
DOI : 10.1016/j.str.2005.09.020
URL : https://hal.archives-ouvertes.fr/hal-00502073

L. Yatime, E. Schmitt, S. Blanquet, and Y. Mechulam, Functional Molecular Mapping of Archaeal Translation Initiation Factor 2, Journal of Biological Chemistry, vol.279, issue.16, pp.15984-15993, 2004.
DOI : 10.1074/jbc.M311561200
URL : https://hal.archives-ouvertes.fr/hal-00770710

D. Farruggio, J. Chaudhuri, U. Maitra, and U. L. Rajbhandary, The A1 x U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2., Molecular and Cellular Biology, vol.16, issue.8, pp.4248-4256, 1996.
DOI : 10.1128/MCB.16.8.4248

E. Schmitt, S. Blanquet, and Y. Mechulam, The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors, The EMBO Journal, vol.21, issue.7, pp.1821-1832, 2002.
DOI : 10.1093/emboj/21.7.1821
URL : https://hal.archives-ouvertes.fr/hal-00770921

M. Sokabe, M. Yao, N. Sakai, S. Toya, and I. Tanaka, Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region, Proc. Natl Acad. Sci. USA, pp.13016-13021, 2006.

E. Stolboushkina, S. Nikonov, A. Nikulin, U. Blasi, D. J. Manstein et al., Crystal Structure of the Intact Archaeal Translation Initiation Factor 2 Demonstrates Very High Conformational Flexibility in the ??- and ??-Subunits, Journal of Molecular Biology, vol.382, issue.3, pp.680-691, 2008.
DOI : 10.1016/j.jmb.2008.07.039

L. Yatime, Y. Mechulam, S. Blanquet, and E. Schmitt, Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states, Proc. Natl Acad. Sci. USA, pp.18445-18450, 2007.
DOI : 10.1073/pnas.0706784104
URL : https://hal.archives-ouvertes.fr/hal-00767380

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

A. Roll-mecak, P. Alone, C. Cao, T. E. Dever, and S. K. Burley, X-ray Structure of Translation Initiation Factor eIF2??: IMPLICATIONS FOR tRNA AND eIF2?? BINDING, Journal of Biological Chemistry, vol.279, issue.11, pp.10634-10642, 2004.
DOI : 10.1074/jbc.M310418200

E. Schmitt, M. Panvert, C. Lazennec-schurdevin, P. D. Coureux, J. Perez et al., Structure of the ternary initiation complex aIF2???GDPNP???methionylated initiator tRNA, Nature Structural & Molecular Biology, vol.430, issue.4, pp.450-454, 2012.
DOI : 10.1107/S0021889895007047
URL : https://hal.archives-ouvertes.fr/hal-00764443

B. S. Shin, J. R. Kim, S. E. Walker, J. Dong, J. R. Lorsch et al., Initiation factor eIF2?? promotes eIF2???GTP???Met-tRNAiMet ternary complex binding to the 40S ribosome, Nature Structural & Molecular Biology, vol.318, issue.11, pp.1227-1234, 2011.
DOI : 10.1016/S0076-6879(07)30006-2

J. Nika, S. Rippel, and E. M. Hannig, Biochemical Analysis of the eIF2???? Complex Reveals a Structural Function for eIF2?? in Catalyzed Nucleotide Exchange, Journal of Biological Chemistry, vol.276, issue.2, pp.1051-1060, 2001.
DOI : 10.1074/jbc.M007398200

A. Flynn, S. Oldfield, and C. G. Proud, The role of the beta-subunit of initiation factor eIF-2 in initiation complex formation, Biochim. Biophys. Acta, pp.1174-117, 1993.

Y. Mechulam, L. Guillon, L. Yatime, S. Blanquet, and E. Schmitt, Protection-Based Assays to Measure Aminoacyl-tRNA Binding to Translation Initiation Factors, Methods Enzymol, vol.430, pp.265-281, 2007.
DOI : 10.1016/S0076-6879(07)30011-6
URL : https://hal.archives-ouvertes.fr/hal-00502061

J. M. Guillon, T. Meinnel, Y. Mechulam, C. Lazennec, S. Blanquet et al., Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAfMet formyltransferase, Journal of Molecular Biology, vol.224, issue.2, pp.359-367, 1992.
DOI : 10.1016/0022-2836(92)91000-F

T. Meinnel and S. Blanquet, Maturation of pre-tRNA fMet by E. coli RNase P is specified by a guanosine of the 5 0 flanking sequence, J. Biol. Chem, vol.270, pp.15906-15914, 1995.

P. Mellot, Y. Mechulam, D. Lecorre, S. Blanquet, and G. Fayat, Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition, Journal of Molecular Biology, vol.208, issue.3, pp.429-443, 1989.
DOI : 10.1016/0022-2836(89)90507-X

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. David and J. Perez, Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline, Journal of Applied Crystallography, vol.42, issue.5, pp.892-900, 2009.
DOI : 10.1107/S0021889809029288

P. V. Konarev, V. V. Volkov, M. V. Petoukhov, and D. I. Svergun, 2.1, a program package for small-angle scattering data analysis, Journal of Applied Crystallography, vol.39, issue.2, pp.277-286, 2006.
DOI : 10.1107/S0021889806004699

D. I. Svergun, C. Barberato, and M. H. Koch, ??? a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates, Journal of Applied Crystallography, vol.28, issue.6, pp.768-773, 1995.
DOI : 10.1107/S0021889895007047

T. Wagner, M. Gross, and P. B. Sigler, Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis, J. Biol. Chem, vol.259, pp.4706-4709, 1984.

L. D. Kapp, S. E. Kolitz, and J. R. Lorsch, Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation, RNA, vol.12, issue.5, pp.751-764, 2006.
DOI : 10.1261/rna.2263906

T. Ito, A. Marintchev, and G. Wagner, Solution Structure of Human Initiation Factor eIF2?? Reveals Homology to the Elongation Factor eEF1B, Structure, vol.12, issue.9, pp.1693-1704, 2004.
DOI : 10.1016/j.str.2004.07.010

N. N. Hashimoto, L. S. Carnevalli, and B. A. Castilho, Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits, Biochemical Journal, vol.367, issue.2, pp.359-368, 2002.
DOI : 10.1042/bj20020556

A. G. Hinnebusch and J. R. Lorsch, The Mechanism of Eukaryotic Translation Initiation: New Insights and Challenges, Cold Spring Harbor Perspectives in Biology, vol.4, issue.10, 2012.
DOI : 10.1101/cshperspect.a011544

T. F. Donahue, A. M. Cigan, E. K. Pabich, and B. C. Valavicius, Mutations at a Zn(II) finger motif in the yeast elF-2?? gene alter ribosomal start-site selection during the scanning process, Cell, vol.54, issue.5, pp.621-632, 1988.
DOI : 10.1016/S0092-8674(88)80006-0

A. M. Cigan, E. K. Pabich, L. Feng, and T. F. Donahue, Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit., Proc. Natl Acad. Sci. USA, pp.2784-2788, 1989.
DOI : 10.1073/pnas.86.8.2784