메뉴 건너뛰기




Volumn 18, Issue 3, 2012, Pages 421-433

The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10,catalyze the formation of 1-methylpseudouridine at position 54 of tRNA

Author keywords

Archaea; Haloferax volcanii; TrmY; tRNA methylation; tRNA modification

Indexed keywords

1 METHYLPSEUDOURIDINE; ARCHAEAL PROTEIN; METHYLTRANSFERASE; PROTEIN COG1901; PSEUDOURIDINE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84857387516     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.030841.111     Document Type: Article
Times cited : (33)

References (65)
  • 2
    • 2342625231 scopus 로고    scopus 로고
    • Development of Additional Selectable Markers for the Halophilic Archaeon Haloferax volcanii Based on the leuB and trpA Genes
    • DOI 10.1128/AEM.70.2.943-953.2004
    • Allers T, Ngo H, Mevarech M, Lloyd RG. 2004. Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes. Appl Environ Microbiol 70: 943-953. (Pubitemid 38568219)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.2 , pp. 943-953
    • Allers, T.1    Ngo, H.-P.2    Mevarech, M.3    Lloyd, R.G.4
  • 5
    • 0032245524 scopus 로고    scopus 로고
    • Mapping of pseudouridine residues in RNA to nucleotide resolution
    • Bakin AV, Ofengand J. 1998. Mapping of pseudouridine residues in RNA to nucleotide resolution. Methods Mol Biol 77: 297-309.
    • (1998) Methods Mol Biol , vol.77 , pp. 297-309
    • Bakin, A.V.1    Ofengand, J.2
  • 6
    • 0031565927 scopus 로고    scopus 로고
    • Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the Tψ-loop of yeast tRNAs
    • DOI 10.1006/jmbi.1997.1417
    • Becker HF, Motorin Y, Sissler M, Florentz C, Grosjean H. 1997. Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the T ψ-loop of yeast tRNAs. J Mol Biol 274: 505-518. (Pubitemid 28004664)
    • (1997) Journal of Molecular Biology , vol.274 , Issue.4 , pp. 505-518
    • Becker, H.F.1    Motorin, Y.2    Sissler, M.3    Florentz, C.4    Grosjean, H.5
  • 7
    • 0017877962 scopus 로고
    • Composition and characterization of tRNA from Methanococcus vannielii
    • Best AN. 1978. Composition and characterization of tRNA from Methanococcus vannielii. J Bacteriol 133: 240-250. (Pubitemid 8259447)
    • (1978) Journal of Bacteriology , vol.133 , Issue.1 , pp. 240-250
    • Best, A.N.1
  • 8
    • 79952132927 scopus 로고    scopus 로고
    • Towards a systems approach in the genetic analysis of archaea: Accelerating mutant construction and phenotypic analysis in Haloferax volcanii
    • doi: 10.1155/2010/426239
    • Blaby IK, Phillips G, Blaby-Haas CE, Gulig KS, El Yacoubi B, de Crécy-Lagard V. 2010. Towards a systems approach in the genetic analysis of archaea: accelerating mutant construction and phenotypic analysis in Haloferax volcanii. Archaea 2010: 426239. doi: 10.1155/2010/426239.
    • (2010) Archaea , vol.2010 , pp. 426239
    • Blaby, I.K.1    Phillips, G.2    Blaby-Haas, C.E.3    Gulig, K.S.4    El Yacoubi, B.5    De Crécy-Lagard, V.6
  • 9
    • 0017802149 scopus 로고
    • Biosynthesis of a hypermodified nucleotide in Saccharomyces carlsbergensis 17S and HeLa-cell 18S ribosomal ribonucleic acid
    • Brand RC, Klootwijk J, Planta RJ, Maden BE. 1978. Biosynthesis of a hypermodified nucleotide in Saccharomyces carlsbergensis 17S and HeLa-cell 18S ribosomal ribonucleic acid. Biochem J 169: 71-77. (Pubitemid 8270563)
    • (1978) Biochemical Journal , vol.169 , Issue.1 , pp. 71-77
    • Brand, R.C.1    Klootwijk, J.2    Planta, R.J.3    Maden, B.E.H.4
  • 10
    • 33747617329 scopus 로고    scopus 로고
    • Genetic evidence for 18S rRNA binding and an Rps19p assembly function of yeast nucleolar protein Nep1p
    • DOI 10.1007/s00438-006-0132-x
    • Buchhaupt M, Meyer B, Kötter P, Entian K-D. 2006. Genetic evidence for 18S rRNA binding and an Rps19p assembly function of yeast nucleolar protein Nep1p. Mol Genet Genomics 276: 273-284. (Pubitemid 44268037)
    • (2006) Molecular Genetics and Genomics , vol.276 , Issue.3 , pp. 273-284
    • Buchhaupt, M.1    Meyer, B.2    Kotter, P.3    Entian, K.-D.4
  • 12
    • 79951483622 scopus 로고    scopus 로고
    • Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase
    • Chen H-Y, Yuan YA. 2010. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J Mol Cell Biol 2: 366-374.
    • (2010) J Mol Cell Biol , vol.2 , pp. 366-374
    • Chen, H.-Y.1    Yuan, Y.A.2
  • 14
    • 0033105160 scopus 로고    scopus 로고
    • Transfer RNA modification enzymes from Pyrococcus furiosus: Detection of the enzymatic activities in vitro
    • DOI 10.1093/nar/27.5.1308
    • Constantinesco F, Motorin Y, Grosjean H. 1999. Transfer RNA modification enzymes from Pyrococcus furiosus: detection of the enzymatic activities in vitro. Nucleic Acids Res 27: 1308-1315. (Pubitemid 29206440)
    • (1999) Nucleic Acids Research , vol.27 , Issue.5 , pp. 1308-1315
    • Constantinesco, F.1    Motorin, Y.2    Grosjean, H.3
  • 15
    • 0025683270 scopus 로고
    • Preparation and enzymatic hydrolysis of DNA and RNA for mass spectrometry
    • Crain PF. 1990. Preparation and enzymatic hydrolysis of DNA and RNA for mass spectrometry. Methods Enzymol 193: 782-790.
    • (1990) Methods Enzymol , vol.193 , pp. 782-790
    • Crain, P.F.1
  • 18
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797. (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 19
    • 0022432563 scopus 로고
    • Thermospray liquid chromatography-mass spectrometry of nucleosides and of enzymatic hydrolysates of nucleic acids
    • Edmonds CG, Vestal ML, McCloskey JA. 1985. Thermospray liquid chromatography-mass spectrometry of nucleosides and of enzymatic hydrolysates of nucleic acids. Nucleic Acids Res 13: 8197-8206.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8197-8206
    • Edmonds, C.G.1    Vestal, M.L.2    McCloskey, J.A.3
  • 21
    • 85075274229 scopus 로고    scopus 로고
    • Nucleic Acids are not boring long polymers of only four types of nucleotides
    • (ed. H Grosjean), Landes Bioscience, Austin, TX
    • Grosjean H. 2009. Nucleic Acids are not boring long polymers of only four types of nucleotides. In DNA and RNA modification enzymes: Structure, mechanism, function and evolution (ed. H Grosjean), pp. 1-18. Landes Bioscience, Austin, TX.
    • (2009) DNA and RNA Modification Enzymes: Structure, Mechanism, Function and Evolution , pp. 1-18
    • Grosjean, H.1
  • 22
    • 0028884401 scopus 로고
    • A novel enzymatic pathway leading to 1-methylinosine modification in Haloferax volcanii tRNA
    • Grosjean H, Constantinesco F, Foiret D, Benachenhou N. 1995. A novel enzymatic pathway leading to 1-methylinosine modification in Haloferax volcanii tRNA. Nucleic Acids Res 23: 4312-4319.
    • (1995) Nucleic Acids Res , vol.23 , pp. 4312-4319
    • Grosjean, H.1    Constantinesco, F.2    Foiret, D.3    Benachenhou, N.4
  • 23
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • DOI 10.1006/jmbi.1996.0007
    • Grosjean H, Edqvist J, Straby KB, Giegé R. 1996. Enzymatic formation of modified nucleosides in tRNA: dependence on tRNA architecture. J Mol Biol 255: 67-85. (Pubitemid 26104185)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.1 , pp. 67-85
    • Grosjean, H.1    Edqvist, J.2    Straby, K.B.3    Giege, R.4
  • 24
    • 34548801413 scopus 로고    scopus 로고
    • Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates
    • Grosjean H, Droogmans L, Roovers M, Keith G. 2007. Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates. Methods Enzymol 425: 55-101.
    • (2007) Methods Enzymol , vol.425 , pp. 55-101
    • Grosjean, H.1    Droogmans, L.2    Roovers, M.3    Keith, G.4
  • 25
    • 56349150890 scopus 로고    scopus 로고
    • RNomics and Modomics in the halophilic archaea Haloferax volcanii: Identification of RNA modification genes
    • doi: 10.1186/1471-2164-9-470
    • Grosjean H, Gaspin C, Marck C, Decatur WA, de Crécy-Lagard V. 2008a. RNomics and Modomics in the halophilic archaea Haloferax volcanii: identification of RNA modification genes. BMC Genomics 9: 470. doi: 10.1186/1471-2164-9-470.
    • (2008) BMC Genomics , vol.9 , pp. 470
    • Grosjean, H.1    Gaspin, C.2    Marck, C.3    Decatur, W.A.4    De Crécy-Lagard, V.5
  • 26
    • 55749111501 scopus 로고    scopus 로고
    • Modified nucleotides in Archaeal RNAs
    • (ed. P Blum), Horizon Scientific Press, Caister Academic Press, Cambridge, UK
    • Grosjean H, Gupta R, Maxwell ES. 2008b. Modified nucleotides in Archaeal RNAs. In Archaea: New models for prokaryotic biology (ed. P Blum), pp. 171-196. Horizon Scientific Press, Caister Academic Press, Cambridge, UK.
    • (2008) Archaea: New Models for Prokaryotic Biology , pp. 171-196
    • Grosjean, H.1    Gupta, R.2    Maxwell, E.S.3
  • 27
    • 0021112528 scopus 로고
    • Sequences of halobacterial tRNAs and the paucity of U in the first position of their anticodons
    • Gu X-R, Nicoghosian K, Cedergren RJ, Wong JT-F. 1983. Sequences of halobacterial tRNAs and the paucity of U in the first position of their anticodons. Nucleic Acids Res 11: 5433-5442.
    • (1983) Nucleic Acids Res , vol.11 , pp. 5433-5442
    • Gu, X.-R.1    Nicoghosian, K.2    Cedergren, R.J.3    Wong, J.T.-F.4
  • 28
    • 0006838919 scopus 로고
    • Glycine and asparagme tRNA sequences from the archaebacteriuin, Methanobacterium thermoautotrophicum
    • Gu X-R, Nicoghosian K, Cedergren RJ. 1984. Glycine and asparagme tRNA sequences from the archaebacteriuin, Methanobacterium thermoautotrophicum. FEBS Lett 176: 462-466.
    • (1984) FEBS Lett , vol.176 , pp. 462-466
    • Gu, X.-R.1    Nicoghosian, K.2    Cedergren, R.J.3
  • 29
    • 0029786633 scopus 로고    scopus 로고
    • 5U54)- methyltransferase is not sequence specific
    • DOI 10.1021/bi9612125
    • Gu X, Ivanetich KM, Santi DV. 1996. Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase is not sequence specific. Biochemistry 35: 11652-11659. (Pubitemid 26303682)
    • (1996) Biochemistry , vol.35 , Issue.36 , pp. 11652-11659
    • Gu, X.1    Ivanetich, K.M.2    Santi, D.V.3
  • 30
    • 0021153752 scopus 로고
    • Halobacterium volcanii tRNAs. Identification of 41 tRNAs covering all amino acids, and the sequences of 33 class I tRNAs
    • Gupta R. 1984. Halobacterium volcanii tRNAs: identification of 41 tRNAs covering all amino acids, and the sequences of 33 Class I tRNAs. J Biol Chem 259: 9461-9471. (Pubitemid 14060506)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.15 , pp. 9461-9471
    • Gupta, R.1
  • 31
    • 0022529031 scopus 로고
    • Transfer RNAs of Halobacterium volcanii: Sequences of five leucine and three serine tRNAs
    • Gupta R. 1986. Transfer RNAs of Halobacterium volcanii: sequences of five leucine and three serine tRNAs. Syst Appl Microbiol 7: 102-105. (Pubitemid 16079303)
    • (1986) Systematic and Applied Microbiology , vol.7 , Issue.1 , pp. 102-105
    • Gupta, R.1
  • 32
    • 0019162933 scopus 로고
    • Unusual modification patterns in the transfer ribonucleic acids of archaebacteria
    • Gupta R, Woese C. 1980. Unusual modification patterns in the transfer ribonucleic acids of archaebacteria. Curr Microbiol 4: 245-249. (Pubitemid 11170092)
    • (1980) Current Microbiology , vol.4 , Issue.4 , pp. 245-249
    • Gupta, R.1    Woese, C.R.2
  • 33
    • 57049151350 scopus 로고    scopus 로고
    • Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in tRNA
    • Gurha P, Gupta R. 2008. Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in tRNA. RNA 14: 2521-2527.
    • (2008) RNA , vol.14 , pp. 2521-2527
    • Gurha, P.1    Gupta, R.2
  • 34
    • 36248957607 scopus 로고    scopus 로고
    • Differential roles of archaeal box H/ACA proteins in guide RNA-dependent and independent pseudouridine formation
    • Gurha P, Joardar A, Chaurasia P, Gupta R. 2007. Differential roles of archaeal box H/ACA proteins in guide RNA-dependent and independent pseudouridine formation. RNA Biol 4: 101-109. (Pubitemid 350127834)
    • (2007) RNA Biology , vol.4 , Issue.2 , pp. 101-109
    • Gurha, P.1    Joardar, A.2    Chaurasia, P.3    Gupta, R.4
  • 35
    • 0034547125 scopus 로고    scopus 로고
    • Deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells
    • DOI 10.1017/S1355838200001588
    • Gutgsell N, Englund N, Niu L, Kaya Y, Lane BG, Ofengand J. 2000. Deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells. RNA 6: 1870-1881. (Pubitemid 32001956)
    • (2000) RNA , vol.6 , Issue.12 , pp. 1870-1881
    • Gutgsell, N.1    Englund, N.2    Niu, L.3    Kaya, Y.4    Lane, B.G.5    Ofengand, J.6
  • 37
  • 38
    • 0036855267 scopus 로고    scopus 로고
    • Physiological analysis of the role of truB in Escherichia coli: A role for tRNA modification in extreme temperature resistance
    • Kinghorn SM, O'Byrne CP, Booth IR, Stansfield I. 2002. Physiological analysis of the role of truB in Escherichia coli: a role for tRNA modification in extreme temperature resistance. Microbiology 148: 3511-3520. (Pubitemid 35414461)
    • (2002) Microbiology , vol.148 , Issue.11 , pp. 3511-3520
    • Kinghorn, S.M.1    O'Byrne, C.P.2    Booth, I.R.3    Stansfield, I.4
  • 39
    • 34548839373 scopus 로고    scopus 로고
    • Active Suppressor tRNAs with a Double Helix between the D- and T-loops
    • DOI 10.1016/j.jmb.2007.07.058, PII S0022283607010236
    • Kotlova N, Ishii TM, Zagryadskaya EI, Steinberg SV. 2007. Active suppressor tRNAs with a double helix between the D- and T-loops. J Mol Biol 373: 462-475. (Pubitemid 47445569)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.2 , pp. 462-475
    • Kotlova, N.1    Ishii, T.M.2    Zagryadskaya, E.I.3    Steinberg, S.V.4
  • 40
    • 0028272470 scopus 로고
    • The role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles
    • DOI 10.1021/bi00191a014
    • Kowalak JA, Dalluge JJ, McCloskey JA, Stetter KO. 1994. The role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles. Biochemistry 33: 7869-7876. (Pubitemid 24223805)
    • (1994) Biochemistry , vol.33 , Issue.25 , pp. 7869-7876
    • Kowalak, J.A.1    Dalluge, J.J.2    McCloskey, J.A.3    Stetter, K.O.4
  • 41
    • 0034637542 scopus 로고    scopus 로고
    • Identities and phylogenetic comparisons of posttranscriptional modifications in 16 S ribosomal RNA from Haloferax volcanii
    • DOI 10.1074/jbc.M002153200
    • Kowalak JA, Bruenger E, Crain PF, McCloskey JA. 2000. Identities and phylogenetic comparisons of posttranscriptional modifications in 16S ribosomal RNA from Haloferax volcanii. J Biol Chem 275: 24484-24489. (Pubitemid 30626541)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24484-24489
    • Kowalak, J.A.1    Bruenger, E.2    Crain, P.F.3    McCloskey, J.A.4
  • 42
    • 0020050750 scopus 로고
    • Initiator tRNAs from archaebacteria show common unique sequence characteristics
    • DOI 10.1038/298684a0
    • Kuchino Y, Ihara M, Yabusaki Y, Nishimura S. 1982. Initiator tRNAs from archaebacteria show common unique sequence characteristics. Nature 298: 684-685. (Pubitemid 12099733)
    • (1982) Nature , vol.298 , Issue.5875 , pp. 684-685
    • Kuchino, Y.1    Ihara, M.2    Yabusaki, Y.3    Nishimura, S.4
  • 43
    • 14844293080 scopus 로고    scopus 로고
    • A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function
    • DOI 10.1016/j.cell.2004.12.037
    • Lee TT, Agarwalla S, Stroud RM. 2005. A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Cell 120: 599-611. (Pubitemid 40343073)
    • (2005) Cell , vol.120 , Issue.5 , pp. 599-611
    • Lee, T.T.1    Agarwalla, S.2    Stroud, R.M.3
  • 44
    • 39149096592 scopus 로고    scopus 로고
    • The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases
    • DOI 10.1093/nar/gkm1074
    • Leulliot N, Bohnsack MT, Graille M, Tollervey D, Van Tilbeurgh H. 2008. The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of α/β knot fold methyltransferases. Nucleic Acids Res 36: 629-639. (Pubitemid 351255435)
    • (2008) Nucleic Acids Research , vol.36 , Issue.2 , pp. 629-639
    • Leulliot, N.1    Bohnsack, M.T.2    Graille, M.3    Tollervey, D.4    Van Tilbeurgh, H.5
  • 45
    • 0036792830 scopus 로고    scopus 로고
    • TRNomics: Analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodonsparing strategies and domain-specific features
    • Marck C, Grosjean H. 2002. tRNomics: analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodonsparing strategies and domain-specific features. RNA 8: 1189-1232.
    • (2002) RNA , vol.8 , pp. 1189-1232
    • Marck, C.1    Grosjean, H.2
  • 46
    • 79952331212 scopus 로고    scopus 로고
    • The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of C1191 in yeast 18S rRNA
    • Meyer B, Wurm JP, Kötter P, Leisegang MS, Schilling V, Buchhaupt M, Held M, Bahr U, Karas M, Heckel A, et al. 2011. The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of C1191 in yeast 18S rRNA. Nucleic Acids Res 39: 1526-1537.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1526-1537
    • Meyer, B.1    Wurm, J.P.2    Kötter, P.3    Leisegang, M.S.4    Schilling, V.5    Buchhaupt, M.6    Held, M.7    Bahr, U.8    Karas, M.9    Heckel, A.10
  • 48
    • 34548726200 scopus 로고    scopus 로고
    • Identification of modified residues in RNAs by reverse transcription-based methods
    • Motorin Y, Muller S, Behm-Ansmant I, Branlant C. 2007. Identification of modified residues in RNAs by reverse transcription-based methods. Methods Enzymol 425: 21-53.
    • (2007) Methods Enzymol , vol.425 , pp. 21-53
    • Motorin, Y.1    Muller, S.2    Behm-Ansmant, I.3    Branlant, C.4
  • 49
    • 0022368898 scopus 로고
    • Halobacterium cutirubrum tRNA sequences
    • DOI 10.1016/0014-5793(85)80164-2
    • Nicoghosian K, Gu X-R, Cedergren R. 1985. Halobacterium cutirubrum tRNA sequences. FEBS Lett 193: 255-260. (Pubitemid 16163994)
    • (1985) FEBS Letters , vol.193 , Issue.2 , pp. 255-260
    • Nicoghosian, K.1    Gu, X.-R.2    Cedergren, R.3
  • 50
    • 0019880102 scopus 로고
    • RNA processing in microinjected Xenopus oocytes. Sequential addition of base modifications in the spliced transfer RNA
    • Nishikura K, De Robertis EM. 1981. RNA processing in microinjected Xenopus oocytes. Sequential addition of base modifications in the spliced transfer RNA. J Mol Biol 145: 405-420.
    • (1981) J Mol Biol , vol.145 , pp. 405-420
    • Nishikura, K.1    De Robertis, E.M.2
  • 52
    • 0018974885 scopus 로고
    • Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic acid (5-methyluridine)-methyltransferase in Escherichia coli K-12
    • Ny T, Björk GR. 1980. Cloning and restriction mapping of the trmA gene coding for transfer ribonucleic acid (5-methyluridine)-methyltransferase in Escherichia coli K-12. J Bacteriol 142: 371-379. (Pubitemid 10044919)
    • (1980) Journal of Bacteriology , vol.142 , Issue.2 , pp. 371-379
    • Ny, T.1    Bjork, G.R.2
  • 53
    • 0035721651 scopus 로고    scopus 로고
    • Mapping pseudouridines in RNA molecules
    • DOI 10.1006/meth.2001.1249
    • Ofengand J, Del Campo M, Kaya Y. 2001. Mapping pseudouridines in RNA molecules. Methods 25: 365-373. (Pubitemid 34183561)
    • (2001) Methods , vol.25 , Issue.3 , pp. 365-373
    • Ofengand, J.1    Del, C.M.2    Kaya, Y.3
  • 55
    • 0020478845 scopus 로고
    • Structure of a modified nucleoside in archaebacterial tRNA which replaces ribosylthymine. 1-Methylpseudouridine
    • Pang H, Ihara M, Kuchino Y, Nishimura S, Gupta R, Woese CR, McCloskey JA. 1982. Structure of a modified nucleoside in archaebacterial tRNA which replaces ribosylthymine. 1-Methylpseudouridine. J Biol Chem 257: 3589-3592.
    • (1982) J Biol Chem , vol.257 , pp. 3589-3592
    • Pang, H.1    Ihara, M.2    Kuchino, Y.3    Nishimura, S.4    Gupta, R.5    Woese, C.R.6    McCloskey, J.A.7
  • 57
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • DOI 10.1093/bioinformatics/btg180
    • Ronquist F, Huelsenbeck JP. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574. (Pubitemid 37038874)
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 59
    • 41149170790 scopus 로고    scopus 로고
    • The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site
    • DOI 10.1093/nar/gkm1172
    • Taylor AB, Meyer B, Leal BZ, Kötter P, Schirf V, Demeler B, Hart PJ, Entian K-D, Wöhnert J. 2008. The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site. Nucleic Acids Res 36: 1542-1554. (Pubitemid 351426107)
    • (2008) Nucleic Acids Research , vol.36 , Issue.5 , pp. 1542-1554
    • Taylor, A.B.1    Meyer, B.2    Leal, B.Z.3    Kotter, P.4    Schirf, V.5    Demeler, B.6    Hart, P.J.7    Entian, K.-D.8    Wohnert, J.9
  • 60
    • 79953683436 scopus 로고    scopus 로고
    • Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis
    • Thomas SR, Keller CA, Szyk A, Cannon JR, LaRonde-LeBlanc NA. 2011. Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis. Nucleic Acids Res 39: 2445-2457.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2445-2457
    • Thomas, S.R.1    Keller, C.A.2    Szyk, A.3    Cannon, J.R.4    LaRonde-LeBlanc, N.A.5
  • 61
    • 34648820435 scopus 로고    scopus 로고
    • Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases
    • doi: 10.1186/1471-2105-8-73
    • Tkaczuk K, Dunin-Horkawicz S, Purta E, Bujnicki J. 2007. Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases. BMC Bioinformatics 8: 73. doi: 10.1186/1471-2105-8-73.
    • (2007) BMC Bioinformatics , vol.8 , pp. 73
    • Tkaczuk, K.1    Dunin-Horkawicz, S.2    Purta, E.3    Bujnicki, J.4
  • 62
    • 37349022099 scopus 로고    scopus 로고
    • Acquisition of a bacterial RumA-type tRNA(uracil-54, C5)- methyltransferase by Archaea through an ancient horizontal gene transfer
    • DOI 10.1111/j.1365-2958.2007.06047.x
    • Urbonavicius J, Auxilien S, Walbott H, Trachana K, Golinelli-Pimpaneau B, Brochier-Armanet C, Grosjean H. 2008. Acquisition of a bacterial RumA-type tRNA(uracil-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer. Mol Microbiol 67: 323-335. (Pubitemid 350295838)
    • (2008) Molecular Microbiology , vol.67 , Issue.2 , pp. 323-335
    • Urbonavicius, J.1    Auxilien, S.2    Walbott, H.3    Trachana, K.4    Golinelli-Pimpaneau, B.5    Brochier-Armanet, C.6    Grosjean, H.7
  • 63
    • 50849135134 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity
    • Walbott H, Leulliot N, Grosjean H, Golinelli-Pimpaneau B. 2008. The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity. Nucleic Acids Res 36: 4929-4940.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4929-4940
    • Walbott, H.1    Leulliot, N.2    Grosjean, H.3    Golinelli-Pimpaneau, B.4
  • 65
    • 0019876752 scopus 로고
    • A sequence from Drosophila melanogaster 18S rRNA bearing the conserved hypermodified nucleoside amψ: Analysis by reverse transcription and high-performance liquid chromatography
    • Youvan DC, Hearst JE. 1981. A sequence from Drosophila melanogaster 18S rRNA bearing the conserved hypermodified nucleoside amψ: analysis by reverse transcription and high-performance liquid chromatography. Nucleic Acids Res 9: 1723-1742.
    • (1981) Nucleic Acids Res , vol.9 , pp. 1723-1742
    • Youvan, D.C.1    Hearst, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.