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Volumn 2, Issue 1, 2007, Pages

Optimization of ribosome structure and function by rRNA base modification

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; PEPTIDYLTRANSFERASE; RIBOSOME RNA; TRANSFER RNA;

EID: 34249868208     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0000174     Document Type: Article
Times cited : (118)

References (49)
  • 1
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289: 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 0032894591 scopus 로고    scopus 로고
    • A comprehensive database for the small nucleolar RNAs from Saccharomyces cerevisiae
    • Samarsky DA, Fournier MJ (1999) A comprehensive database for the small nucleolar RNAs from Saccharomyces cerevisiae. Nucleic Acids Res 27: 161-164.
    • (1999) Nucleic Acids Res , vol.27 , pp. 161-164
    • Samarsky, D.A.1    Fournier, M.J.2
  • 4
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur WA, Fournier MJ (2002) rRNA modifications and ribosome function. Trends Biochem Sci 27: 344-351.
    • (2002) Trends Biochem Sci , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 6
    • 0029903805 scopus 로고    scopus 로고
    • In vitro complementation analysis localizes 23S rRNA posttranscriptional modifications that are required for Escherichia coli 50S ribosomal subunit assembly and function
    • Green R, Noller HF (1996) In vitro complementation analysis localizes 23S rRNA posttranscriptional modifications that are required for Escherichia coli 50S ribosomal subunit assembly and function. RNA 2: 1011-1021.
    • (1996) RNA , vol.2 , pp. 1011-1021
    • Green, R.1    Noller, H.F.2
  • 7
    • 0027536869 scopus 로고
    • Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly
    • Tollervey D, Lehtonen H, Jansen R, Kern H, Hurt EC (1993) Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. Cell 72: 443-457.
    • (1993) Cell , vol.72 , pp. 443-457
    • Tollervey, D.1    Lehtonen, H.2    Jansen, R.3    Kern, H.4    Hurt, E.C.5
  • 8
    • 0032718276 scopus 로고    scopus 로고
    • Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA
    • Zebarjadian Y, King T, Fournier MJ, Clarke L, Carbon J (1999) Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. Mol Cell Biol 19: 7461-7472.
    • (1999) Mol Cell Biol , vol.19 , pp. 7461-7472
    • Zebarjadian, Y.1    King, T.2    Fournier, M.J.3    Clarke, L.4    Carbon, J.5
  • 9
    • 0033582628 scopus 로고    scopus 로고
    • A computational screen for methylation guide snoRNAs in yeast
    • Lowe TM, Eddy SR (1999) A computational screen for methylation guide snoRNAs in yeast. Science 283: 1168-1171.
    • (1999) Science , vol.283 , pp. 1168-1171
    • Lowe, T.M.1    Eddy, S.R.2
  • 10
    • 0031787478 scopus 로고    scopus 로고
    • A pseudouridine synthase required for the formation of two universally conserved pseudouridines in ribosomal RNA is essential for normal growth of Escherichia coli
    • Raychaudhuri S, Conrad J, Hall BG, Ofengand J (1998) A pseudouridine synthase required for the formation of two universally conserved pseudouridines in ribosomal RNA is essential for normal growth of Escherichia coli. RNA 4: 1407-1417.
    • (1998) RNA , vol.4 , pp. 1407-1417
    • Raychaudhuri, S.1    Conrad, J.2    Hall, B.G.3    Ofengand, J.4
  • 11
    • 0033516555 scopus 로고    scopus 로고
    • Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA
    • Raychaudhuri S, Niu L, Conrad J, Lane BG, Ofengand J (1999) Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA. J Biol Chem 274: 18880-18886.
    • (1999) J Biol Chem , vol.274 , pp. 18880-18886
    • Raychaudhuri, S.1    Niu, L.2    Conrad, J.3    Lane, B.G.4    Ofengand, J.5
  • 12
    • 0033935223 scopus 로고    scopus 로고
    • Pseudouridine in RNA: What, where, how, and why
    • Charette M, Gray MW (2000) Pseudouridine in RNA: what, where, how, and why. IUBMB Life 49: 341-351.
    • (2000) IUBMB Life , vol.49 , pp. 341-351
    • Charette, M.1    Gray, M.W.2
  • 13
    • 32644447756 scopus 로고    scopus 로고
    • Post-transcriptional nucleotide modification and alternative folding of RNA
    • Helm M (2006) Post-transcriptional nucleotide modification and alternative folding of RNA. Nucleic Acids Res 34: 721-733.
    • (2006) Nucleic Acids Res , vol.34 , pp. 721-733
    • Helm, M.1
  • 14
    • 0034744390 scopus 로고    scopus 로고
    • Thermodynamics of 2′-ribose substitutions in UUCG tetraloops
    • Williams DJ, Boots JL, Hall KB (2001) Thermodynamics of 2′-ribose substitutions in UUCG tetraloops. RNA 7: 44-53.
    • (2001) RNA , vol.7 , pp. 44-53
    • Williams, D.J.1    Boots, J.L.2    Hall, K.B.3
  • 15
    • 0034657608 scopus 로고    scopus 로고
    • Unique structural and stabilizing roles for the individual pseudouridine residues in the 1920 region of Escherichia coli 23S rRNA
    • Meroueh M, Grohar PJ, Qiu J, SantaLucia J Jr, Scaringe SA, et al. (2000) Unique structural and stabilizing roles for the individual pseudouridine residues in the 1920 region of Escherichia coli 23S rRNA. Nucleic Acids Res 28: 2075-2083.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2075-2083
    • Meroueh, M.1    Grohar, P.J.2    Qiu, J.3    SantaLucia Jr, J.4    Scaringe, S.A.5
  • 16
    • 24044454056 scopus 로고    scopus 로고
    • Effects of nucleotide substitution and modification on the stability and structure of helix 69 from 28S rRNA
    • Sumita M, Desaulniers JP, Chang YC, Chui HM, Clos L, et al. (2005) Effects of nucleotide substitution and modification on the stability and structure of helix 69 from 28S rRNA. RNA 11: 1420-1429.
    • (2005) RNA , vol.11 , pp. 1420-1429
    • Sumita, M.1    Desaulniers, J.P.2    Chang, Y.C.3    Chui, H.M.4    Clos, L.5
  • 17
    • 0031912037 scopus 로고    scopus 로고
    • Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant
    • Gustafsson C, Persson BC (1998) Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant. J Bacteriol 180: 359-365.
    • (1998) J Bacteriol , vol.180 , pp. 359-365
    • Gustafsson, C.1    Persson, B.C.2
  • 18
    • 0037292453 scopus 로고    scopus 로고
    • Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center
    • King TH, Liu B, McCully RR, Fournier MJ (2003) Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center. Molecular Cell 11: 425-435.
    • (2003) Molecular Cell , vol.11 , pp. 425-435
    • King, T.H.1    Liu, B.2    McCully, R.R.3    Fournier, M.J.4
  • 19
    • 0345276473 scopus 로고    scopus 로고
    • Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2′-O-ribose methylation of a conserved rRNA position in yeast
    • Bonnerot C, Pintard L, Lutfalla G (2003) Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2′-O-ribose methylation of a conserved rRNA position in yeast. Molecular Cell 12: 1309-1315.
    • (2003) Molecular Cell , vol.12 , pp. 1309-1315
    • Bonnerot, C.1    Pintard, L.2    Lutfalla, G.3
  • 20
    • 8844219672 scopus 로고    scopus 로고
    • Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage
    • Lapeyre B, Purushothaman SK (2004) Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage. Mol Cell 16: 663-669.
    • (2004) Mol Cell , vol.16 , pp. 663-669
    • Lapeyre, B.1    Purushothaman, S.K.2
  • 21
    • 0034596029 scopus 로고    scopus 로고
    • The FtsJ/ RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase
    • Caldas T, Binet E, Bouloc P, Costa A, Desgres J, et al. (2000) The FtsJ/ RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase. J Biol Chem 275: 16414-16419.
    • (2000) J Biol Chem , vol.275 , pp. 16414-16419
    • Caldas, T.1    Binet, E.2    Bouloc, P.3    Costa, A.4    Desgres, J.5
  • 24
    • 0015877247 scopus 로고
    • The tricodermin group of antibiotics, inhibitors of peptide bond formation by eukaryotic ribosomes
    • Carrasco L, Barbacid M, Vazquez D (1973) The tricodermin group of antibiotics, inhibitors of peptide bond formation by eukaryotic ribosomes. Biochim et Biophys Acta 312: 368-376.
    • (1973) Biochim et Biophys Acta , vol.312 , pp. 368-376
    • Carrasco, L.1    Barbacid, M.2    Vazquez, D.3
  • 25
    • 0014198715 scopus 로고
    • Inhibitors of protein biosynthesis. II. Mode of action of anisomycin
    • Grollman AP (1967) Inhibitors of protein biosynthesis. II. Mode of action of anisomycin. J Biol Chem 242: 3226-3233.
    • (1967) J Biol Chem , vol.242 , pp. 3226-3233
    • Grollman, A.P.1
  • 26
    • 0016330482 scopus 로고
    • Two classes of inhibitors of peptidyltransferase activity in eukaryotes
    • Schindler D (1974) Two classes of inhibitors of peptidyltransferase activity in eukaryotes. Nature 249: 38-41.
    • (1974) Nature , vol.249 , pp. 38-41
    • Schindler, D.1
  • 27
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen JL, Moore PB, Steitz TA (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol 330: 1061-1075.
    • (2003) J Mol Biol , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 28
    • 0014501228 scopus 로고
    • Stabilization of N-acetylphenylalanyl transfer ribonucleic acid binding to ribosomes by sparsomycin
    • Herner AE, Goldberg IH, Cohen LB (1969) Stabilization of N-acetylphenylalanyl transfer ribonucleic acid binding to ribosomes by sparsomycin. Biochemistry 8: 1335-1344.
    • (1969) Biochemistry , vol.8 , pp. 1335-1344
    • Herner, A.E.1    Goldberg, I.H.2    Cohen, L.B.3
  • 29
    • 0014226040 scopus 로고
    • Localization of sparsomycin action to the peptide-bond-forming step
    • Jayaraman J, Goldberg IH (1968) Localization of sparsomycin action to the peptide-bond-forming step. Biochemistry 7: 418-421.
    • (1968) Biochemistry , vol.7 , pp. 418-421
    • Jayaraman, J.1    Goldberg, I.H.2
  • 30
    • 0025811850 scopus 로고
    • Sites of interaction of the CCA end of peptidyl-tRNA with 23S rRNA
    • Moazed D, Noller HF (1991) Sites of interaction of the CCA end of peptidyl-tRNA with 23S rRNA. Proc Natl Acad Sci U S A 88: 3725-3728.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3725-3728
    • Moazed, D.1    Noller, H.F.2
  • 31
    • 0026643735 scopus 로고
    • 1 double-stranded RNA virus propagation
    • 1 double-stranded RNA virus propagation. J Virology 66: 3669-3676.
    • (1992) J Virology , vol.66 , pp. 3669-3676
    • Dinman, J.D.1    Wickner, R.B.2
  • 32
    • 0029942532 scopus 로고    scopus 로고
    • Double-stranded RNA viruses of Saccharomyces cerevisiae
    • Wickner RB (1996) Double-stranded RNA viruses of Saccharomyces cerevisiae. Microbiol Rev 60: 250-265.
    • (1996) Microbiol Rev , vol.60 , pp. 250-265
    • Wickner, R.B.1
  • 33
    • 0042703890 scopus 로고    scopus 로고
    • An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae
    • Harger JW, Dinman JD (2003) An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae. RNA 9: 1019-1024.
    • (2003) RNA , vol.9 , pp. 1019-1024
    • Harger, J.W.1    Dinman, J.D.2
  • 35
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • Katunin VI, Muth GW, Strobel SA, Wintermeyer W, Rodnina MV (2002) Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome. Mol Cell 10: 339-346.
    • (2002) Mol Cell , vol.10 , pp. 339-346
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 36
    • 27644502679 scopus 로고    scopus 로고
    • Simulating movement of tRNA into the ribosome during decoding
    • Sanbonmatsu KY, Joseph S, Tung CS (2005) Simulating movement of tRNA into the ribosome during decoding. Proc Natl Acad Sci U S A 102: 15854-15859.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15854-15859
    • Sanbonmatsu, K.Y.1    Joseph, S.2    Tung, C.S.3
  • 37
    • 0028032017 scopus 로고
    • Translational maintenance of frame: Mutants of Saccharomyces cerevisiae with altered - 1 ribosomal frameshifting efficiencies
    • Dinman JD, Wickner RB (1994) Translational maintenance of frame: mutants of Saccharomyces cerevisiae with altered - 1 ribosomal frameshifting efficiencies. Genetics 136: 75-86.
    • (1994) Genetics , vol.136 , pp. 75-86
    • Dinman, J.D.1    Wickner, R.B.2
  • 38
    • 0028945414 scopus 로고
    • Yeast virus propagation depends critically on free 60S ribosomal subunit concentration
    • Ohtake Y, Wickner RB (1995) Yeast virus propagation depends critically on free 60S ribosomal subunit concentration. Mol Cell Biol 15: 2772-2781.
    • (1995) Mol Cell Biol , vol.15 , pp. 2772-2781
    • Ohtake, Y.1    Wickner, R.B.2
  • 39
    • 0025303605 scopus 로고
    • Ribosomal frameshifting in the yeast retrotransposon Ty: TRNAs induce slippage on a 7 nucleotide minimal site
    • Belcourt MF, Farabaugh PJ (1990) Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site. Cell 62: 339-352.
    • (1990) Cell , vol.62 , pp. 339-352
    • Belcourt, M.F.1    Farabaugh, P.J.2
  • 40
    • 33745205638 scopus 로고    scopus 로고
    • Conserved loop sequence of helix 69 in Escherichia coli 23 S rRNA is involved in A-site tRNA binding and translational fidelity
    • Hirabayashi N, Sato NS, Suzuki T (2006) Conserved loop sequence of helix 69 in Escherichia coli 23 S rRNA is involved in A-site tRNA binding and translational fidelity. J Biol Chem 281: 17203-17211.
    • (2006) J Biol Chem , vol.281 , pp. 17203-17211
    • Hirabayashi, N.1    Sato, N.S.2    Suzuki, T.3
  • 41
    • 3242656131 scopus 로고    scopus 로고
    • Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing
    • Mochizuki Y, He J, Kulkarni S, Bessler M, Mason PJ (2004) Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing. Proc Natl Acad Sci U S A 101: 10756-10761.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10756-10761
    • Mochizuki, Y.1    He, J.2    Kulkarni, S.3    Bessler, M.4    Mason, P.J.5
  • 42
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita
    • Yoon A, Peng G, Brandenburger Y, Zollo O, Xu W, et al. (2006) Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita. Science 312: 902-906.
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1    Peng, G.2    Brandenburger, Y.3    Zollo, O.4    Xu, W.5
  • 43
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue H, Nojima H, Okayama H (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96: 23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 44
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168.
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 45
    • 16544392668 scopus 로고    scopus 로고
    • Systematic analysis of bicistronic reporter assay data
    • Jacobs JL, Dinman JD (2004) Systematic analysis of bicistronic reporter assay data. Nucleic Acids Res 32: e160-e170.
    • (2004) Nucleic Acids Res , vol.32
    • Jacobs, J.L.1    Dinman, J.D.2
  • 46
    • 0034897729 scopus 로고    scopus 로고
    • Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae
    • Meskauskas A, Dinman JD (2001) Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae. RNA 7: 1084-1096.
    • (2001) RNA , vol.7 , pp. 1084-1096
    • Meskauskas, A.1    Dinman, J.D.2
  • 47
    • 28544434886 scopus 로고    scopus 로고
    • Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis
    • Meskauskas A, Petrov AN, Dinman JD (2005) Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis. Molecular & Cellular Biology 25: 10863-10874.
    • (2005) Molecular & Cellular Biology , vol.25 , pp. 10863-10874
    • Meskauskas, A.1    Petrov, A.N.2    Dinman, J.D.3
  • 49
    • 33845228894 scopus 로고    scopus 로고
    • An arc of unpaired "hinge bases" facilitates information exchange among functional centers of the ribosome
    • Rakauskaite R, Dinman JD (2006) An arc of unpaired "hinge bases" facilitates information exchange among functional centers of the ribosome. Mol Cell Biol 26: 8992-9002.
    • (2006) Mol Cell Biol , vol.26 , pp. 8992-9002
    • Rakauskaite, R.1    Dinman, J.D.2


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