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

URL : https://academic.oup.com/nar/article-pdf/27/1/196/4063413/27-1-196.pdf

W. A. Decatur and M. J. Fournier, rRNA modifications and ribosome function, Trends in Biochemical Sciences, vol.27, issue.7, pp.344-351, 2002.
DOI : 10.1016/S0968-0004(02)02109-6

T. H. King, B. Liu, R. R. Mccully, and M. J. Fournier, Ribosome Structure and Activity Are Altered in Cells Lacking snoRNPs that Form Pseudouridines in the Peptidyl Transferase Center, Molecular Cell, vol.11, issue.2, pp.425-435, 2003.
DOI : 10.1016/S1097-2765(03)00040-6

M. Sumita, J. P. Desaulniers, Y. C. Chang, H. M. Chui, L. Clos et al., Effects of nucleotide substitution and modification on the stability and structure of helix 69 from 28S rRNA, RNA, vol.11, issue.9, pp.1420-1429, 2005.
DOI : 10.1261/rna.2320605

G. Badis, M. Fromont-racine, and A. Jacquier, A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast, RNA, vol.9, issue.7, pp.771-779, 2003.
DOI : 10.1261/rna.5240503

M. Meroueh, P. J. Grohar, J. Qiu, J. Santalucia, . Jr et al., Unique structural and stabilizing roles for the individual pseudouridine residues in the 1920 region of Escherichia coli 23S rRNA, Nucleic Acids Research, vol.28, issue.10, pp.2075-2083, 2000.
DOI : 10.1093/nar/28.10.2075

F. Kirpekar, L. H. Hansen, A. Rasmussen, J. Poehlsgaard, and B. Vester, The Archaeon Haloarcula marismortui has Few Modifications in the Central Parts of its 23S Ribosomal RNA, Journal of Molecular Biology, vol.348, issue.3, pp.563-573, 2005.
DOI : 10.1016/j.jmb.2005.03.009

D. Campo, M. Recinos, C. Yanez, G. Pomerantz, S. C. Guymon et al., Number, position, and significance of the pseudouridines in the large subunit ribosomal RNA of Haloarcula marismortui and Deinococcus radiodurans, RNA, vol.11, issue.2, pp.210-219, 2005.
DOI : 10.1261/rna.7209905

Y. T. Yu, M. D. Shu, and J. A. Steitz, Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing, The EMBO Journal, vol.17, issue.19, pp.5783-5795, 1998.
DOI : 10.1093/emboj/17.19.5783

T. Hamma and A. R. Ferre-d-'amare, Pseudouridine Synthases, Chemistry & Biology, vol.13, issue.11, pp.1125-1135, 2006.
DOI : 10.1016/j.chembiol.2006.09.009

URL : https://doi.org/10.1016/j.chembiol.2006.09.009

H. O. Kammen, C. C. Marvel, L. Hardy, and E. E. Penhoet, Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I, J. Biol. Chem, vol.263, pp.2255-2263, 1988.

K. Nurse, J. Wrzesinski, A. Bakin, B. G. Lane, and J. Ofengand, Purification, cloning, and properties of the tRNA Psi 55 synthase from Escherichia coli, RNA, vol.1, pp.102-112, 1995.

J. Wrzesinski, A. Bakin, K. Nurse, B. G. Lane, and J. Ofengand, Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli, Biochemistry, vol.34, issue.27, pp.8904-8913, 1995.
DOI : 10.1021/bi00027a043

J. Wrzesinski, K. Nurse, A. Bakin, B. G. Lane, and J. Ofengand, A dual-specificity pseudouridine synthase: An Escherichia coli synthase purified and cloned on the basis of its specificity for É746 in 23S RNA is also specific for É32 in tRNA phe, RNA, vol.1, pp.437-448, 1995.

E. V. Koonin, Pseudouridine Synthases: Four Families of Enzymes Containing a Putative Uridine-Binding Motif Also Conserved in dUTPases and dCTP Deaminases, Nucleic Acids Research, vol.24, issue.12, pp.2411-2415, 1996.
DOI : 10.1093/nar/24.12.2411

Y. Kaya and J. Ofengand, A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya, RNA, vol.9, issue.6, pp.711-721, 2003.
DOI : 10.1261/rna.5230603

I. Behm-ansmant, A. Urban, X. Ma, Y. Yu, Y. Motorin et al., The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:??-synthase also acting on tRNAs, RNA, vol.9, issue.11, pp.1371-1382, 2003.
DOI : 10.1261/rna.5520403

M. Del-campo, J. Ofengand, and A. Malhotra, Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli, RNA, vol.10, issue.2, pp.231-239, 2004.
DOI : 10.1261/rna.5187404

Y. Kaya, D. Campo, M. Ofengand, J. Malhotra, and A. , Crystal Structure of TruD, a Novel Pseudouridine Synthase with a New Protein Fold, Journal of Biological Chemistry, vol.10, issue.18, pp.18107-18110, 2004.
DOI : 10.1107/S0907444999010495

V. Ramamurthy, S. L. Swann, J. L. Paulson, C. J. Spedaliere, and E. G. Mueller, Critical Aspartic Acid Residues in Pseudouridine Synthases, Journal of Biological Chemistry, vol.11, issue.32, pp.22225-22230, 1999.
DOI : 10.1017/S1355838298980761

URL : http://www.jbc.org/content/274/32/22225.full.pdf

J. Conrad, L. Niu, K. Rudd, B. G. Lane, and J. Ofengand, 16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: Deletion, mutation of the conserved Asp102 residue, and sequence comparison among all other pseudouridine synthases, RNA, vol.5, issue.6, pp.761-763, 1999.
DOI : 10.1017/S1355838299990167

S. Raychaudhuri, L. Niu, J. Conrad, B. G. Lane, and J. Ofengand, Ribosomal RNA and tRNA Pseudouridine Synthase RluA, Journal of Biological Chemistry, vol.171, issue.27, pp.18880-18886, 1999.
DOI : 10.1073/pnas.89.9.3995

A. R. Ferre-d-'amare, RNA-modifying enzymes, Current Opinion in Structural Biology, vol.13, issue.1, pp.49-55, 2003.
DOI : 10.1016/S0959-440X(02)00002-7

L. Aravind and E. V. Koonin, Novel Predicted RNA-Binding Domains Associated with the Translation Machinery, Journal of Molecular Evolution, vol.48, issue.3, pp.291-302, 1999.
DOI : 10.1007/PL00006472

X. Manival, C. Charron, J. B. Fourmann, F. Godard, B. Charpentier et al., Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity, Nucleic Acids Research, vol.34, issue.3, pp.826-839, 2006.
DOI : 10.1093/nar/gkj482

T. Hamma, S. L. Reichow, G. Varani, and A. R. Ferre-d-'amare, The Cbf5???Nop10 complex is a molecular bracket that organizes box H/ACA RNPs, Nature Structural & Molecular Biology, vol.148, issue.12, pp.1101-1107, 2005.
DOI : 10.1016/j.jsb.2004.06.010

R. Rashid, B. Liang, D. L. Baker, O. A. Youssef, Y. He et al., Crystal Structure of a Cbf5-Nop10-Gar1 Complex and Implications in RNA-Guided Pseudouridylation and Dyskeratosis Congenita, Molecular Cell, vol.21, issue.2, pp.249-260, 2006.
DOI : 10.1016/j.molcel.2005.11.017

L. Li and K. Ye, Crystal structure of an H/ACA box ribonucleoprotein particle, Nature, vol.100, issue.7109, pp.302-307, 2006.
DOI : 10.1073/pnas.2135585100

C. Hoang and A. R. Ferre-d-'amare, Cocrystal Structure of a tRNA ??55 Pseudouridine Synthase, Cell, vol.107, issue.7, pp.929-939, 2001.
DOI : 10.1016/S0092-8674(01)00618-3

J. P. Bachellerie, J. Cavaille, and A. Huttenhofer, The expanding snoRNA world, Biochimie, vol.84, issue.8, pp.775-790, 2002.
DOI : 10.1016/S0300-9084(02)01402-5

T. Kiss, Small Nucleolar RNAs, Cell, vol.109, issue.2, pp.145-148, 2002.
DOI : 10.1016/S0092-8674(02)00718-3

A. D. Omer, S. Ziesche, W. A. Decatur, M. J. Fournier, and P. P. Dennis, RNA-modifying machines in archaea, Molecular Microbiology, vol.292, issue.3, pp.617-629, 2003.
DOI : 10.1128/MCB.12.6.2561

URL : http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2003.03483.x/pdf

D. L. Baker, O. A. Youssef, M. I. Chastkofsky, D. A. Dy, R. M. Terns et al., RNA-Guided RNA modification: functional organization of the archaeal H/ACA RNP, Genes & Development, vol.19, issue.10, pp.1238-1248, 2005.
DOI : 10.1101/gad.1309605

B. Charpentier, S. Muller, and C. Branlant, Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation, Nucleic Acids Research, vol.33, issue.10, pp.3133-3144, 2005.
DOI : 10.1093/nar/gki630

URL : https://hal.archives-ouvertes.fr/hal-01662780

M. Khanna, H. Wu, C. Johansson, M. Caizergues-ferrer, and J. Feigon, Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA, RNA, vol.12, issue.1, pp.40-52, 2006.
DOI : 10.1261/rna.2221606

URL : https://hal.archives-ouvertes.fr/hal-00109511

T. S. Rozhdestvensky, T. H. Tang, I. V. Tchirkova, J. Brosius, J. P. Bachellerie et al., Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif Nucleic Acids Research, p.5623, 2003.

T. Hamma and A. R. Ferre-d-'amare, Structure of Protein L7Ae Bound to a K-Turn Derived from an Archaeal Box H/ACA sRNA at 1.8 ?? Resolution, Structure, vol.12, issue.5, pp.893-903, 2004.
DOI : 10.1016/j.str.2004.03.015

M. Roovers, C. Hale, C. Tricot, M. P. Terns, R. M. Terns et al., Formation of the conserved pseudouridine at position 55 in archaeal tRNA, Nucleic Acids Research, vol.34, issue.15, pp.4293-4301, 2006.
DOI : 10.1093/nar/gkl530

B. Charpentier, J. B. Fourmann, and C. Branlant, Reconstitution of Archaeal H/ACA sRNPs and Test of their Activity, Methods Enzymol, vol.425, pp.389-405, 2007.
DOI : 10.1016/S0076-6879(07)25016-5

A. Bakin and J. Ofengand, Four newly located pseudouridylate residues in Escherichia coli 23S ribosomal RNA are all at the peptidyltransferase center: Analysis by the application of a new sequencing technique, Biochemistry, vol.32, issue.37, pp.9754-9762, 1993.
DOI : 10.1021/bi00088a030

A. Mougin, A. Gregoire, J. Banroques, V. Segault, R. Fournier et al., Secondary structure of the yeast Saccharomyces cerevisiae pre-U3A snoRNA and its implication for splicing efficiency, RNA, vol.2, pp.1079-1093, 1996.

Y. Motorin, S. Muller, I. Behm-ansmant, and C. Branlant, Identification of Modified Residues in RNAs by Reverse Transcription???Based Methods, Methods Enzymol, vol.425, pp.21-53, 2007.
DOI : 10.1016/S0076-6879(07)25002-5

H. Jin, J. P. Loria, and P. B. Moore, Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA, Molecular Cell, vol.26, issue.2, pp.205-215, 2007.
DOI : 10.1016/j.molcel.2007.03.014

H. Wu and J. Feigon, H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification, Proc. Natl Acad. Sci. USA, pp.6655-6660, 2007.
DOI : 10.1016/0263-7855(96)00009-4

K. Tomita, R. Ishitani, S. Fukai, and O. Nureki, Complete crystallographic analysis of the dynamics of CCA sequence addition, Nature, vol.54, issue.7114, pp.956-960, 2006.
DOI : 10.1107/S0907444998003254

C. Wang and U. T. Meier, Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins, The EMBO Journal, vol.19, issue.8, pp.1857-1867, 2004.
DOI : 10.1038/sj.emboj.7600181

H. Pan, S. Agarwalla, D. T. Moustakas, J. Finer-moore, and R. M. Stroud, Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit, Proc. Natl Acad. Sci. USA, pp.12648-12653, 2003.
DOI : 10.1093/protein/8.2.127

Y. Zebarjadian, T. King, M. J. Fournier, L. Clarke, and J. Carbon, Can Abolish In Vivo Pseudouridylation of rRNA, Molecular and Cellular Biology, vol.19, issue.11, pp.7461-7472, 1999.
DOI : 10.1128/MCB.19.11.7461

A. G. Russell, M. N. Schnare, and M. W. Gray, Pseudouridine-guide RNAs and other Cbf5p-associated RNAs in Euglena gracilis, RNA, vol.10, issue.7, pp.1034-1046, 2004.
DOI : 10.1261/rna.7300804