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Volumn 425, Issue , 2007, Pages 283-316

Identifying Effects of snoRNA-Guided Modifications on the Synthesis and Function of the Yeast Ribosome

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYL GROUP; NUCLEOTIDE; PSEUDOURIDINE; RIBOSOME RNA; SMALL NUCLEOLAR RIBONUCLEOPROTEIN; SMALL NUCLEOLAR RNA; URIDINE DERIVATIVE;

EID: 34548751838     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)25013-X     Document Type: Review
Times cited : (30)

References (150)
  • 2
    • 33745621079 scopus 로고    scopus 로고
    • Probing the secondary structure of expansion segment ES6 in 18S ribosomal RNA
    • Alkemar G., and Nygard O. Probing the secondary structure of expansion segment ES6 in 18S ribosomal RNA. Biochemistry (Mosc.) 45 (2006) 8067-8078
    • (2006) Biochemistry (Mosc.) , vol.45 , pp. 8067-8078
    • Alkemar, G.1    Nygard, O.2
  • 3
    • 0038721061 scopus 로고    scopus 로고
    • A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast
    • Badis G., Fromont-Racine M., and Jacquier A. A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast. RNA 9 (2003) 771-779
    • (2003) RNA , vol.9 , pp. 771-779
    • Badis, G.1    Fromont-Racine, M.2    Jacquier, A.3
  • 4
    • 0021822441 scopus 로고
    • A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c
    • Baim S.B., Pietras D.F., Eustice D.C., and Sherman F. A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol. 5 (1985) 1839-1846
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1839-1846
    • Baim, S.B.1    Pietras, D.F.2    Eustice, D.C.3    Sherman, F.4
  • 5
    • 0027440297 scopus 로고
    • snR31, snR32, and snR33: Three novel, non-essential snRNAs from Saccharomyces cerevisiae
    • Balakin A.G., Schneider G.S., Corbett M.S., Ni J., and Fournier M.J. snR31, snR32, and snR33: Three novel, non-essential snRNAs from Saccharomyces cerevisiae. Nucleic Acids Res. 21 (1993) 5391-5397
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5391-5397
    • Balakin, A.G.1    Schneider, G.S.2    Corbett, M.S.3    Ni, J.4    Fournier, M.J.5
  • 6
    • 0030572699 scopus 로고    scopus 로고
    • The RNA world of the nucleolus: Two major families of small RNAs defined by different box elements with related functions
    • Balakin A.G., Smith L., and Fournier M.J. The RNA world of the nucleolus: Two major families of small RNAs defined by different box elements with related functions. Cell 86 (1996) 823-834
    • (1996) Cell , vol.86 , pp. 823-834
    • Balakin, A.G.1    Smith, L.2    Fournier, M.J.3
  • 7
    • 0032519508 scopus 로고    scopus 로고
    • A chemical modification method for the structural analysis of RNA and RNA-protein complexes within living cells
    • Balzer M., and Wagner R. A chemical modification method for the structural analysis of RNA and RNA-protein complexes within living cells. Anal. Biochem. 256 (1998) 240-242
    • (1998) Anal. Biochem. , vol.256 , pp. 240-242
    • Balzer, M.1    Wagner, R.2
  • 8
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., and Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289 (2000) 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
  • 9
    • 0031897326 scopus 로고    scopus 로고
    • Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis
    • Benard L., Carroll K., Valle R.C., and Wickner R.B. Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis. Mol. Cell. Biol. 18 (1998) 2688-2696
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2688-2696
    • Benard, L.1    Carroll, K.2    Valle, R.C.3    Wickner, R.B.4
  • 10
    • 0028302637 scopus 로고
    • Synthetic lethality with fibrillarin identifies Nop77p, a nucleolar protein required for pre-rRNA processing and modification
    • Berges T., Petfalski E., Tollervey D., and Hurt E.C. Synthetic lethality with fibrillarin identifies Nop77p, a nucleolar protein required for pre-rRNA processing and modification. EMBO J. 13 (1994) 3136-3148
    • (1994) EMBO J. , vol.13 , pp. 3136-3148
    • Berges, T.1    Petfalski, E.2    Tollervey, D.3    Hurt, E.C.4
  • 12
    • 0035137890 scopus 로고    scopus 로고
    • Endless possibilities: Translation termination and stop codon recognition
    • Bertram G., Innes S., Minella O., Richardson J., and Stansfield I. Endless possibilities: Translation termination and stop codon recognition. Microbiology 147 (2001) 255-269
    • (2001) Microbiology , vol.147 , pp. 255-269
    • Bertram, G.1    Innes, S.2    Minella, O.3    Richardson, J.4    Stansfield, I.5
  • 13
    • 4544382906 scopus 로고    scopus 로고
    • The snoRNPs and Related Machines: Ancient Devices That Mediate Maturation of rRNA and Other RNAs
    • Olson M.O.J. (Ed), Eurekah.com and Kluwer Academic/Plenum Publishers, Georgetown, TX; New York, NY
    • Bertrand E., and Fournier M.J. The snoRNPs and Related Machines: Ancient Devices That Mediate Maturation of rRNA and Other RNAs. In: Olson M.O.J. (Ed). "The Nucleolus" (2004), Eurekah.com and Kluwer Academic/Plenum Publishers, Georgetown, TX; New York, NY 223-257
    • (2004) "The Nucleolus" , pp. 223-257
    • Bertrand, E.1    Fournier, M.J.2
  • 14
    • 0033942924 scopus 로고    scopus 로고
    • Nonsense-mediated decay mutants do not affect programmed -1 frameshifting
    • Bidou L., Stahl G., Hatin I., Namy O., Rousset J.P., and Farabaugh P.J. Nonsense-mediated decay mutants do not affect programmed -1 frameshifting. RNA 6 (2000) 952-961
    • (2000) RNA , vol.6 , pp. 952-961
    • Bidou, L.1    Stahl, G.2    Hatin, I.3    Namy, O.4    Rousset, J.P.5    Farabaugh, P.J.6
  • 15
    • 0029153552 scopus 로고
    • The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae
    • Bonetti B., Fu L., Moon J., and Bedwell D.M. The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae. J. Mol. Biol. 251 (1995) 334-345
    • (1995) J. Mol. Biol. , vol.251 , pp. 334-345
    • Bonetti, B.1    Fu, L.2    Moon, J.3    Bedwell, D.M.4
  • 16
    • 0033555266 scopus 로고    scopus 로고
    • Elements essential for accumulation and function of small nucleolar RNAs directing site-specific pseudouridylation of ribosomal RNAs
    • Bortolin M.L., Ganot P., and Kiss T. Elements essential for accumulation and function of small nucleolar RNAs directing site-specific pseudouridylation of ribosomal RNAs. EMBO J. 18 (1999) 457-469
    • (1999) EMBO J. , vol.18 , pp. 457-469
    • Bortolin, M.L.1    Ganot, P.2    Kiss, T.3
  • 17
    • 0036816641 scopus 로고    scopus 로고
    • Probing the structural dynamics of nucleic acids by quantitative time-resolved and equilibrium hydroxyl radical "footprinting."
    • Brenowitz M., Chance M.R., Dhavan G., and Takamoto K. Probing the structural dynamics of nucleic acids by quantitative time-resolved and equilibrium hydroxyl radical "footprinting.". Curr. Opin. Struct. Biol. 12 (2002) 648-653
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 648-653
    • Brenowitz, M.1    Chance, M.R.2    Dhavan, G.3    Takamoto, K.4
  • 18
    • 0034669350 scopus 로고    scopus 로고
    • Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor
    • Briones C., and Ballesta J.P. Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor. Nucleic Acids Res. 28 (2000) 4497-4505
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4497-4505
    • Briones, C.1    Ballesta, J.P.2
  • 19
    • 0033610787 scopus 로고    scopus 로고
    • The GTPase center protein L12 is required for correct ribosomal stalk assembly but not for Saccharomyces cerevisiae viability
    • Briones E., Briones C., Remacha M., and Ballesta J.P. The GTPase center protein L12 is required for correct ribosomal stalk assembly but not for Saccharomyces cerevisiae viability. J. Biol. Chem. 273 (1998) 31956-31961
    • (1998) J. Biol. Chem. , vol.273 , pp. 31956-31961
    • Briones, E.1    Briones, C.2    Remacha, M.3    Ballesta, J.P.4
  • 20
    • 0033654522 scopus 로고    scopus 로고
    • Probing RNA structure and RNA-ligand complexes with chemical probes
    • Brunel C., and Romby P. Probing RNA structure and RNA-ligand complexes with chemical probes. Methods Enzymol. 318 (2000) 3-21
    • (2000) Methods Enzymol. , vol.318 , pp. 3-21
    • Brunel, C.1    Romby, P.2
  • 21
    • 33747617329 scopus 로고    scopus 로고
    • Genetic evidence for 18S rRNA binding and an Rps19p assembly function of yeast nucleolar protein Nep1p
    • Buchhaupt M., Meyer B., Kotter P., and Entian K.D. Genetic evidence for 18S rRNA binding and an Rps19p assembly function of yeast nucleolar protein Nep1p. Mol. Genet. Genomics 276 (2006) 273-284
    • (2006) Mol. Genet. Genomics , vol.276 , pp. 273-284
    • Buchhaupt, M.1    Meyer, B.2    Kotter, P.3    Entian, K.D.4
  • 23
    • 0029919357 scopus 로고    scopus 로고
    • Processing of the intron-encoded U16 and U18 snoRNAs: The conserved C and D boxes control both the processing reaction and the stability of the mature snoRNA
    • Caffarelli E., Fatica A., Prislei S., De Gregorio E., Fragapane P., and Bozzoni I. Processing of the intron-encoded U16 and U18 snoRNAs: The conserved C and D boxes control both the processing reaction and the stability of the mature snoRNA. EMBO J. 15 (1996) 1121-1131
    • (1996) EMBO J. , vol.15 , pp. 1121-1131
    • Caffarelli, E.1    Fatica, A.2    Prislei, S.3    De Gregorio, E.4    Fragapane, P.5    Bozzoni, I.6
  • 24
    • 0029826456 scopus 로고    scopus 로고
    • Processing of fibrillarin-associated snoRNAs from pre-mRNA introns: An exonucleolytic process exclusively directed by the common stem-box terminal structure
    • Cavaille J., and Bachellerie J.P. Processing of fibrillarin-associated snoRNAs from pre-mRNA introns: An exonucleolytic process exclusively directed by the common stem-box terminal structure. Biochimie 78 (1996) 443-456
    • (1996) Biochimie , vol.78 , pp. 443-456
    • Cavaille, J.1    Bachellerie, J.P.2
  • 25
    • 0038120874 scopus 로고    scopus 로고
    • The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli
    • Charollais J., Pflieger D., Vinh J., Dreyfus M., and Iost I. The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli. Mol. Microbiol. 48 (2003) 1253-1265
    • (2003) Mol. Microbiol. , vol.48 , pp. 1253-1265
    • Charollais, J.1    Pflieger, D.2    Vinh, J.3    Dreyfus, M.4    Iost, I.5
  • 26
    • 21744448013 scopus 로고    scopus 로고
    • Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation
    • Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., and Jean-Jean O. Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation. Mol. Cell Biol. 25 (2005) 5801-5811
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5801-5811
    • Chauvin, C.1    Salhi, S.2    Le Goff, C.3    Viranaicken, W.4    Diop, D.5    Jean-Jean, O.6
  • 27
    • 0030614360 scopus 로고    scopus 로고
    • Requirement of the DEAD-box protein ded1p for messenger RNA translation
    • Chuang R.Y., Weaver P.L., Liu Z., and Chang T.H. Requirement of the DEAD-box protein ded1p for messenger RNA translation. Science 275 (1997) 1468-1471
    • (1997) Science , vol.275 , pp. 1468-1471
    • Chuang, R.Y.1    Weaver, P.L.2    Liu, Z.3    Chang, T.H.4
  • 28
    • 1642354169 scopus 로고    scopus 로고
    • Isolation of antibiotic resistance mutations in the rRNA by using an in vitro selection system
    • Cochella L., and Green R. Isolation of antibiotic resistance mutations in the rRNA by using an in vitro selection system. Proc. Natl. Acad. Sci. USA 101 (2004) 3786-3791
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3786-3791
    • Cochella, L.1    Green, R.2
  • 29
    • 33644784770 scopus 로고    scopus 로고
    • Accumulation of unstable promoter-associated transcripts upon loss of the nuclear exosome subunit Rrp6p in Saccharomyces cerevisiae
    • Davis C.A., and Ares Jr. M. Accumulation of unstable promoter-associated transcripts upon loss of the nuclear exosome subunit Rrp6p in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 103 (2006) 3262-3267
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3262-3267
    • Davis, C.A.1    Ares Jr., M.2
  • 30
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur W.A., and Fournier M.J. rRNA modifications and ribosome function. Trends Biochem. Sci. 27 (2002) 344-351
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 31
    • 27844495652 scopus 로고    scopus 로고
    • Small non-coding RNAs in Archaea
    • Dennis P.P., and Omer A. Small non-coding RNAs in Archaea. Curr. Opin. Microbiol. 8 (2005) 685-694
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 685-694
    • Dennis, P.P.1    Omer, A.2
  • 32
    • 0029597787 scopus 로고
    • Multiple regions of yeast ribosomal protein L1 are important for its interaction with 5 S rRNA and assembly into ribosomes
    • Deshmukh M., Stark J., Yeh L.C., Lee J.C., and Woolford Jr. J.L. Multiple regions of yeast ribosomal protein L1 are important for its interaction with 5 S rRNA and assembly into ribosomes. J. Biol. Chem. 270 (1995) 30148-30156
    • (1995) J. Biol. Chem. , vol.270 , pp. 30148-30156
    • Deshmukh, M.1    Stark, J.2    Yeh, L.C.3    Lee, J.C.4    Woolford Jr., J.L.5
  • 33
    • 0030817938 scopus 로고    scopus 로고
    • Translational misreading: Mutations in translation elongation factor 1alpha differentially affect programmed ribosomal frameshifting and drug sensitivity
    • Dinman J.D., and Kinzy T.G. Translational misreading: Mutations in translation elongation factor 1alpha differentially affect programmed ribosomal frameshifting and drug sensitivity. RNA 3 (1997) 870-881
    • (1997) RNA , vol.3 , pp. 870-881
    • Dinman, J.D.1    Kinzy, T.G.2
  • 34
    • 0034691271 scopus 로고    scopus 로고
    • Yeast ribosomal protein L24 affects the kinetics of protein synthesis and ribosomal protein L39 improves translational accuracy, while mutants lacking both remain viable
    • Dresios J., Derkatch I.L., Liebman S.W., and Synetos D. Yeast ribosomal protein L24 affects the kinetics of protein synthesis and ribosomal protein L39 improves translational accuracy, while mutants lacking both remain viable. Biochemistry (Mosc.) 39 (2000) 7236-7244
    • (2000) Biochemistry (Mosc.) , vol.39 , pp. 7236-7244
    • Dresios, J.1    Derkatch, I.L.2    Liebman, S.W.3    Synetos, D.4
  • 36
    • 1942488149 scopus 로고    scopus 로고
    • Has1p, a member of the DEAD-box family, is required for 40S ribosomal subunit biogenesis in Saccharomyces cerevisiae
    • Emery B., de la Cruz J., Rocak S., Deloche O., and Linder P. Has1p, a member of the DEAD-box family, is required for 40S ribosomal subunit biogenesis in Saccharomyces cerevisiae. Mol. Microbiol. 52 (2004) 141-158
    • (2004) Mol. Microbiol. , vol.52 , pp. 141-158
    • Emery, B.1    de la Cruz, J.2    Rocak, S.3    Deloche, O.4    Linder, P.5
  • 37
    • 0036184160 scopus 로고    scopus 로고
    • Ssf1p prevents premature processing of an early pre-60S ribosomal particle
    • Fatica A., Cronshaw A.D., Dlakic M., and Tollervey D. Ssf1p prevents premature processing of an early pre-60S ribosomal particle. Mol. Cell 9 (2002) 341-351
    • (2002) Mol. Cell , vol.9 , pp. 341-351
    • Fatica, A.1    Cronshaw, A.D.2    Dlakic, M.3    Tollervey, D.4
  • 38
    • 0345305424 scopus 로고    scopus 로고
    • Cic1p/Nsa3p is required for synthesis and nuclear export of 60S ribosomal subunits
    • Fatica A., Oeffinger M., Tollervey D., and Bozzoni I. Cic1p/Nsa3p is required for synthesis and nuclear export of 60S ribosomal subunits. RNA 9 (2003) 1431-1436
    • (2003) RNA , vol.9 , pp. 1431-1436
    • Fatica, A.1    Oeffinger, M.2    Tollervey, D.3    Bozzoni, I.4
  • 40
    • 0037387229 scopus 로고    scopus 로고
    • Insights into the structure and function of a guide RNP
    • Fatica A., and Tollervey D. Insights into the structure and function of a guide RNP. Nat. Struct. Biol. 10 (2003) 237-239
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 237-239
    • Fatica, A.1    Tollervey, D.2
  • 41
    • 26944450063 scopus 로고    scopus 로고
    • Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function
    • Ferreira-Cerca S., Poll G., Gleizes P.E., Tschochner H., and Milkereit P. Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function. Mol. Cell 20 (2005) 263-275
    • (2005) Mol. Cell , vol.20 , pp. 263-275
    • Ferreira-Cerca, S.1    Poll, G.2    Gleizes, P.E.3    Tschochner, H.4    Milkereit, P.5
  • 42
    • 33646537802 scopus 로고    scopus 로고
    • Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes
    • Fleischer T.C., Weaver C.M., McAfee K.J., and Jennings and Link A.J. Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev. 20 (2006) 1294-1307
    • (2006) Genes Dev. , vol.20 , pp. 1294-1307
    • Fleischer, T.C.1    Weaver, C.M.2    McAfee, K.J.3    Jennings and Link, A.J.4
  • 43
    • 0025869164 scopus 로고
    • GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae
    • Foiani M., Cigan A.M., Paddon C.J., Harashima S., and Hinnebusch A.G. GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11 (1991) 3203-3216
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3203-3216
    • Foiani, M.1    Cigan, A.M.2    Paddon, C.J.3    Harashima, S.4    Hinnebusch, A.G.5
  • 44
    • 0030698635 scopus 로고    scopus 로고
    • Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis
    • Gautier T., Berges T., Tollervey D., and Hurt E. Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis. Mol. Cell. Biol. 17 (1997) 7088-7098
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7088-7098
    • Gautier, T.1    Berges, T.2    Tollervey, D.3    Hurt, E.4
  • 45
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D., St Jean A., Woods R.A., and Schiestl R.H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20 (1992) 1425
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 46
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz R.D., and Woods R.A. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350 (2002) 87-96
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 47
    • 0037088811 scopus 로고    scopus 로고
    • A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast
    • Gueldener U., Heinisch J., Koehler G.J., Voss D., and Hegemann J.H. A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res. 30 (2002) e23
    • (2002) Nucleic Acids Res. , vol.30
    • Gueldener, U.1    Heinisch, J.2    Koehler, G.J.3    Voss, D.4    Hegemann, J.H.5
  • 48
    • 0034710923 scopus 로고    scopus 로고
    • A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating
    • Guo B., Styles C.A., Feng Q., and Fink G.R. A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating. Proc. Natl. Acad. Sci. USA 97 (2000) 12158-12163
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12158-12163
    • Guo, B.1    Styles, C.A.2    Feng, Q.3    Fink, G.R.4
  • 49
    • 1642276329 scopus 로고    scopus 로고
    • Genetic and epigenetic regulation of the FLO gene family generates cell-surface variation in yeast
    • Halme A., Bumgarner S., Styles C., and Fink G.R. Genetic and epigenetic regulation of the FLO gene family generates cell-surface variation in yeast. Cell 116 (2004) 405-415
    • (2004) Cell , vol.116 , pp. 405-415
    • Halme, A.1    Bumgarner, S.2    Styles, C.3    Fink, G.R.4
  • 50
    • 0028883219 scopus 로고
    • Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4
    • Heilek G.M., Marusak R., Meares C.F., and Noller H.F. Directed hydroxyl radical probing of 16S rRNA using Fe(II) tethered to ribosomal protein S4. Proc. Natl. Acad. Sci. USA 92 (1995) 1113-1116
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1113-1116
    • Heilek, G.M.1    Marusak, R.2    Meares, C.F.3    Noller, H.F.4
  • 51
    • 0019862045 scopus 로고
    • Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide
    • Helser T.L., Baan R.A., and Dahlberg A.E. Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide. Mol. Cell. Biol. 1 (1981) 51-57
    • (1981) Mol. Cell. Biol. , vol.1 , pp. 51-57
    • Helser, T.L.1    Baan, R.A.2    Dahlberg, A.E.3
  • 52
    • 0035107140 scopus 로고    scopus 로고
    • Yeast frameshift suppressor mutations in the genes coding for transcription factor Mbf1p and ribosomal protein S3: Evidence for autoregulation of S3 synthesis
    • Hendrick J.L., Wilson P.G., Edelman I.I., Sandbaken M.G., Ursic D., and Culbertson M.R. Yeast frameshift suppressor mutations in the genes coding for transcription factor Mbf1p and ribosomal protein S3: Evidence for autoregulation of S3 synthesis. Genetics 157 (2001) 1141-1158
    • (2001) Genetics , vol.157 , pp. 1141-1158
    • Hendrick, J.L.1    Wilson, P.G.2    Edelman, I.I.3    Sandbaken, M.G.4    Ursic, D.5    Culbertson, M.R.6
  • 53
    • 0028342849 scopus 로고
    • The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site
    • 24-52-24-63
    • Henry Y., Wood H., Morrissey J.P., Petfalski E., Kearsey S., and Tollervey D. The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site. EMBO J. 13 (1994) 24-52-24-63
    • (1994) EMBO J. , vol.13
    • Henry, Y.1    Wood, H.2    Morrissey, J.P.3    Petfalski, E.4    Kearsey, S.5    Tollervey, D.6
  • 54
    • 20444495201 scopus 로고    scopus 로고
    • Drugs targeting the ribosome
    • Hermann T. Drugs targeting the ribosome. Curr. Opin. Struct. Biol. 15 (2005) 355-366
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 355-366
    • Hermann, T.1
  • 55
    • 33746124556 scopus 로고    scopus 로고
    • Biomolecules in the Computer. Jmol to the Rescue
    • Herráez A. Biomolecules in the Computer. Jmol to the Rescue. Biochem. Mol. Biol. Educ. 34 (2006) 255-261
    • (2006) Biochem. Mol. Biol. Educ. , vol.34 , pp. 255-261
    • Herráez, A.1
  • 56
    • 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 N.S., and Suzuki T. 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 (2006) 17203-17211
    • (2006) J. Biol. Chem. , vol.281 , pp. 17203-17211
    • Hirabayashi, N.1    Sato, N.S.2    Suzuki, T.3
  • 57
    • 0021754243 scopus 로고
    • Probing the conformation of 18S rRNA in yeast 40S ribosomal subunits with kethoxal
    • Hogan J.J., Gutell R.R., and Noller H.F. Probing the conformation of 18S rRNA in yeast 40S ribosomal subunits with kethoxal. Biochemistry (Mosc.) 23 (1984) 3322-3330
    • (1984) Biochemistry (Mosc.) , vol.23 , pp. 3322-3330
    • Hogan, J.J.1    Gutell, R.R.2    Noller, H.F.3
  • 58
    • 0021754238 scopus 로고
    • Probing the conformation of 26S rRNA in yeast 60S ribosomal subunits with kethoxal
    • Hogan J.J., Gutell R.R., and Noller H.F. Probing the conformation of 26S rRNA in yeast 60S ribosomal subunits with kethoxal. Biochemistry (Mosc.) 23 (1984) 3330-3335
    • (1984) Biochemistry (Mosc.) , vol.23 , pp. 3330-3335
    • Hogan, J.J.1    Gutell, R.R.2    Noller, H.F.3
  • 59
    • 0028034493 scopus 로고
    • Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae
    • Iizuka N., Najita L., Franzusoff A., and Sarnow P. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell Biol. 14 (1994) 7322-7330
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7322-7330
    • Iizuka, N.1    Najita, L.2    Franzusoff, A.3    Sarnow, P.4
  • 60
    • 0030993197 scopus 로고    scopus 로고
    • Translation-competent extracts from Saccharomyces cerevisiae: Effects of L-A RNA, 5′ cap, and 3′ poly(A) tail on translational efficiency of mRNAs
    • Iizuka N., and Sarnow P. Translation-competent extracts from Saccharomyces cerevisiae: Effects of L-A RNA, 5′ cap, and 3′ poly(A) tail on translational efficiency of mRNAs. Methods 11 (1997) 353-360
    • (1997) Methods , vol.11 , pp. 353-360
    • Iizuka, N.1    Sarnow, P.2
  • 61
    • 16544392668 scopus 로고    scopus 로고
    • Systematic analysis of bicistronic reporter assay data
    • Jacobs J.L., and Dinman J.D. Systematic analysis of bicistronic reporter assay data. Nucleic Acids Res. 32 (2004) e160
    • (2004) Nucleic Acids Res. , vol.32
    • Jacobs, J.L.1    Dinman, J.D.2
  • 62
    • 0019131495 scopus 로고
    • Expression of a transposable antibiotic resistance element in Saccharomyces
    • Jimenez A., and Davies J. Expression of a transposable antibiotic resistance element in Saccharomyces. Nature 287 (1980) 869-871
    • (1980) Nature , vol.287 , pp. 869-871
    • Jimenez, A.1    Davies, J.2
  • 64
    • 0034769951 scopus 로고    scopus 로고
    • A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins
    • King T.H., Decatur W.A., Bertrand E., Maxwell E.S., and Fournier M.J. A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. Mol. Cell Biol. 21 (2001) 7731-7746
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7731-7746
    • King, T.H.1    Decatur, W.A.2    Bertrand, E.3    Maxwell, E.S.4    Fournier, M.J.5
  • 65
    • 0037292453 scopus 로고    scopus 로고
    • Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center
    • King T.H., Liu B., McCully R.R., and Fournier M.J. Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center. Mol. Cell 11 (2003) 425-435
    • (2003) Mol. Cell , vol.11 , pp. 425-435
    • King, T.H.1    Liu, B.2    McCully, R.R.3    Fournier, M.J.4
  • 66
    • 0029082112 scopus 로고
    • Increased expression of Saccharomyces cerevisiae translation elongation factor 1 alpha bypasses the lethality of a TEF5 null allele encoding elongation factor 1 beta
    • Kinzy, and Woolford. Increased expression of Saccharomyces cerevisiae translation elongation factor 1 alpha bypasses the lethality of a TEF5 null allele encoding elongation factor 1 beta. Genetics 141 (1995) 481-489
    • (1995) Genetics , vol.141 , pp. 481-489
    • Kinzy1    Woolford2
  • 67
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • Klein D.J., Schmeing T.M., Moore P.B., and Steitz T.A. The kink-turn: A new RNA secondary structure motif. EMBO J. 20 (2001) 4214-4221
    • (2001) EMBO J. , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 68
    • 0024841809 scopus 로고
    • Enzymatic approaches to probing of RNA secondary and tertiary structure
    • Knapp G. Enzymatic approaches to probing of RNA secondary and tertiary structure. Methods Enzymol. 180 (1989) 192-212
    • (1989) Methods Enzymol. , vol.180 , pp. 192-212
    • Knapp, G.1
  • 69
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Köhrer K., and Domdey H. Preparation of high molecular weight RNA. Methods Enzymol. 194 (1991) 398-405
    • (1991) Methods Enzymol. , vol.194 , pp. 398-405
    • Köhrer, K.1    Domdey, H.2
  • 70
    • 25844432236 scopus 로고    scopus 로고
    • The putative RNA helicase Dbp4p is required for release of the U14 snoRNA from preribosomes in Saccharomyces cerevisiae
    • Kos M., and Tollervey D. The putative RNA helicase Dbp4p is required for release of the U14 snoRNA from preribosomes in Saccharomyces cerevisiae. Mol. Cell 20 (2005) 53-64
    • (2005) Mol. Cell , vol.20 , pp. 53-64
    • Kos, M.1    Tollervey, D.2
  • 72
    • 0033053360 scopus 로고    scopus 로고
    • Nop58p is a common component of the box C + D snoRNPs that is required for snoRNA stability
    • Lafontaine D.L., and Tollervey D. Nop58p is a common component of the box C + D snoRNPs that is required for snoRNA stability. RNA 5 (1999) 455-467
    • (1999) RNA , vol.5 , pp. 455-467
    • Lafontaine, D.L.1    Tollervey, D.2
  • 73
    • 8844219672 scopus 로고    scopus 로고
    • Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage
    • Lapeyre B., and Purushothaman S.K. Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage. Mol. Cell 16 (2004) 663-669
    • (2004) Mol. Cell , vol.16 , pp. 663-669
    • Lapeyre, B.1    Purushothaman, S.K.2
  • 74
    • 0022422352 scopus 로고
    • Conformation of yeast 18S rRNA. Direct chemical probing of the 5′ domain in ribosomal subunits and in deproteinized RNA by reverse transcriptase mapping of dimethyl sulfate-accessible
    • Lempereur L., Nicoloso M., Riehl N., Ehresmann C., Ehresmann B., and Bachellerie J.P. Conformation of yeast 18S rRNA. Direct chemical probing of the 5′ domain in ribosomal subunits and in deproteinized RNA by reverse transcriptase mapping of dimethyl sulfate-accessible. Nucleic Acids Res. 13 (1985) 8339-8357
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8339-8357
    • Lempereur, L.1    Nicoloso, M.2    Riehl, N.3    Ehresmann, C.4    Ehresmann, B.5    Bachellerie, J.P.6
  • 75
    • 0025166298 scopus 로고
    • Depletion of U14 small nuclear RNA (snR128) disrupts production of 18S rRNA in Saccharomyces cerevisiae
    • Li H.D., Zagorski J., and Fournier M.J. Depletion of U14 small nuclear RNA (snR128) disrupts production of 18S rRNA in Saccharomyces cerevisiae. Mol. Cell Biol. 10 (1990) 1145-1152
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1145-1152
    • Li, H.D.1    Zagorski, J.2    Fournier, M.J.3
  • 76
    • 0036232115 scopus 로고    scopus 로고
    • Lead(II) as a probe for investigating RNA structure in vivo
    • Lindell M., Romby P., and Wagner E.G. Lead(II) as a probe for investigating RNA structure in vivo. RNA 8 (2002) 534-541
    • (2002) RNA , vol.8 , pp. 534-541
    • Lindell, M.1    Romby, P.2    Wagner, E.G.3
  • 77
    • 3042618743 scopus 로고    scopus 로고
    • Interference probing of rRNA with snoRNPs: A novel approach for functional mapping of RNA in vivo
    • Liu B., and Fournier M.J. Interference probing of rRNA with snoRNPs: A novel approach for functional mapping of RNA in vivo. RNA 10 (2004) 1130-1141
    • (2004) RNA , vol.10 , pp. 1130-1141
    • Liu, B.1    Fournier, M.J.2
  • 78
    • 0034852680 scopus 로고    scopus 로고
    • Probing RNA in vivo with methylation guide small nucleolar RNAs
    • Liu B., Ni J., and Fournier M.J. Probing RNA in vivo with methylation guide small nucleolar RNAs. Methods 23 (2001) 276-286
    • (2001) Methods , vol.23 , pp. 276-286
    • Liu, B.1    Ni, J.2    Fournier, M.J.3
  • 79
    • 0033582628 scopus 로고    scopus 로고
    • A computational screen for methylation guide snoRNAs in yeast
    • Lowe T.M., and Eddy S.R. A computational screen for methylation guide snoRNAs in yeast. Science 283 (1999) 1168-1171
    • (1999) Science , vol.283 , pp. 1168-1171
    • Lowe, T.M.1    Eddy, S.R.2
  • 80
    • 22744442531 scopus 로고    scopus 로고
    • Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism
    • Ma X., Yang C., Alexandrov A., Grayhack E.J., Behm-Ansmant I., and Yu Y.T. Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism. EMBO J. 24 (2005) 2403-2413
    • (2005) EMBO J. , vol.24 , pp. 2403-2413
    • Ma, X.1    Yang, C.2    Alexandrov, A.3    Grayhack, E.J.4    Behm-Ansmant, I.5    Yu, Y.T.6
  • 81
    • 0025580878 scopus 로고
    • The numerous modified nucleotides in eukaryotic ribosomal RNA
    • Maden B.E. The numerous modified nucleotides in eukaryotic ribosomal RNA. Prog. Nucleic Acid Res. Mol. Biol. 39 (1990) 241-303
    • (1990) Prog. Nucleic Acid Res. Mol. Biol. , vol.39 , pp. 241-303
    • Maden, B.E.1
  • 83
    • 19444374397 scopus 로고    scopus 로고
    • The many facets of H/ACA ribonucleoproteins
    • Meier U.T. The many facets of H/ACA ribonucleoproteins. Chromosoma 114 (2005) 1-14
    • (2005) Chromosoma , vol.114 , pp. 1-14
    • Meier, U.T.1
  • 84
    • 33745148277 scopus 로고    scopus 로고
    • How a single protein complex accommodates many different H/ACA RNAs
    • Meier U.T. How a single protein complex accommodates many different H/ACA RNAs. Trends Biochem. Sci. 31 (2006) 311-315
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 311-315
    • Meier, U.T.1
  • 85
    • 0031592930 scopus 로고    scopus 로고
    • An in vivo and in vitro structure-function analysis of the Saccharomyces cerevisiae U3A snoRNP: Protein-RNA contacts and base-pair interaction with the pre-ribosomal RNA
    • Mereau A., Fournier R., Gregoire A., Mougin A., Fabrizio P., Luhrmann R., and Branlant C. An in vivo and in vitro structure-function analysis of the Saccharomyces cerevisiae U3A snoRNP: Protein-RNA contacts and base-pair interaction with the pre-ribosomal RNA. J. Mol. Biol. 273 (1997) 552-571
    • (1997) J. Mol. Biol. , vol.273 , pp. 552-571
    • Mereau, A.1    Fournier, R.2    Gregoire, A.3    Mougin, A.4    Fabrizio, P.5    Luhrmann, R.6    Branlant, C.7
  • 86
    • 0034897729 scopus 로고    scopus 로고
    • Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae
    • Meskauskas A., and Dinman J.D. Ribosomal protein L5 helps anchor peptidyl-tRNA to the P-site in Saccharomyces cerevisiae. RNA 7 (2001) 1084-1096
    • (2001) RNA , vol.7 , pp. 1084-1096
    • Meskauskas, A.1    Dinman, J.D.2
  • 87
    • 28544434886 scopus 로고    scopus 로고
    • Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis
    • Meskauskas A., Petrov A.N., and Dinman J.D. Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis. Mol. Cell Biol. 25 (2005) 10863-10874
    • (2005) Mol. Cell Biol. , vol.25 , pp. 10863-10874
    • Meskauskas, A.1    Petrov, A.N.2    Dinman, J.D.3
  • 88
    • 0022470564 scopus 로고
    • Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension
    • Moazed D., Stern S., and Noller H.F. Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension. J. Mol. Biol. 187 (1986) 399-416
    • (1986) J. Mol. Biol. , vol.187 , pp. 399-416
    • Moazed, D.1    Stern, S.2    Noller, H.F.3
  • 89
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • Moore P.B., and Steitz T.A. The structural basis of large ribosomal subunit function. Annu. Rev. Biochem. 72 (2003) 813-850
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 91
    • 0035148955 scopus 로고    scopus 로고
    • Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae
    • Mullen J.R., Kaliraman V., Ibrahim S.S., and Brill S.J. Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae. Genetics 157 (2001) 103-118
    • (2001) Genetics , vol.157 , pp. 103-118
    • Mullen, J.R.1    Kaliraman, V.2    Ibrahim, S.S.3    Brill, S.J.4
  • 92
    • 0034779875 scopus 로고    scopus 로고
    • Impact of the six nucleotides downstream of the stop codon on translation termination
    • Namy O., Hatin I., and Rousset J.P. Impact of the six nucleotides downstream of the stop codon on translation termination. EMBO Rep. 2 (2001) 787-793
    • (2001) EMBO Rep. , vol.2 , pp. 787-793
    • Namy, O.1    Hatin, I.2    Rousset, J.P.3
  • 94
    • 0842267214 scopus 로고    scopus 로고
    • Reprogrammed genetic decoding in cellular gene expression
    • Namy O., Rousset J.P., Napthine S., and Brierley I. Reprogrammed genetic decoding in cellular gene expression. Mol. Cell 13 (2004) 157-168
    • (2004) Mol. Cell , vol.13 , pp. 157-168
    • Namy, O.1    Rousset, J.P.2    Napthine, S.3    Brierley, I.4
  • 95
    • 9644281575 scopus 로고    scopus 로고
    • Ribosomal RNA processing and ribosome biogenesis in eukaryotes
    • Nazar R.N. Ribosomal RNA processing and ribosome biogenesis in eukaryotes. IUBMB Life 56 (2004) 457-465
    • (2004) IUBMB Life , vol.56 , pp. 457-465
    • Nazar, R.N.1
  • 96
    • 0025797364 scopus 로고
    • Synthesis of large rRNAs by RNA polymerase II in mutants of Saccharomyces cerevisiae defective in RNA polymerase I
    • Nogi Y., Yano R., and Nomura M. Synthesis of large rRNAs by RNA polymerase II in mutants of Saccharomyces cerevisiae defective in RNA polymerase I. Proc. Natl. Acad. Sci. USA 88 (1991) 3962-3966
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3962-3966
    • Nogi, Y.1    Yano, R.2    Nomura, M.3
  • 97
    • 33749247285 scopus 로고    scopus 로고
    • Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA
    • Normand C., Capeyrou R., Quevillon-Cheruel S., Mougin A., Henry Y., and Caizergues-Ferrer M. Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA. RNA 12 (2006) 1868-1882
    • (2006) RNA , vol.12 , pp. 1868-1882
    • Normand, C.1    Capeyrou, R.2    Quevillon-Cheruel, S.3    Mougin, A.4    Henry, Y.5    Caizergues-Ferrer, M.6
  • 98
    • 33644955476 scopus 로고    scopus 로고
    • Analysis of the secondary structure of expansion segment 39 in ribosomes from fungi, plants and mammals
    • Nygard O., Alkemar G., and Larsson S.L. Analysis of the secondary structure of expansion segment 39 in ribosomes from fungi, plants and mammals. J. Mol. Biol. 357 (2006) 904-916
    • (2006) J. Mol. Biol. , vol.357 , pp. 904-916
    • Nygard, O.1    Alkemar, G.2    Larsson, S.L.3
  • 99
    • 0027477393 scopus 로고
    • Structural alterations of the nucleolus in mutants of Saccharomyces cerevisiae defective in RNA polymerase I
    • Oakes M., Nogi Y., Clark M.W., and Nomura M. Structural alterations of the nucleolus in mutants of Saccharomyces cerevisiae defective in RNA polymerase I. Mol. Cell Biol. 13 (1993) 2441-2455
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2441-2455
    • Oakes, M.1    Nogi, Y.2    Clark, M.W.3    Nomura, M.4
  • 100
    • 0031581856 scopus 로고    scopus 로고
    • Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria and chloroplasts
    • Ofengand J., and Bakin A. Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria and chloroplasts. J. Mol. Biol. 266 (1997) 246-268
    • (1997) J. Mol. Biol. , vol.266 , pp. 246-268
    • Ofengand, J.1    Bakin, A.2
  • 101
    • 0002387035 scopus 로고    scopus 로고
    • The pseudouridine residues of ribosomal RNA: Number, location, biosynthesis, and function
    • Grosjean H., and Benne R. (Eds), ASM Press, Washington, DC
    • Ofengand J., and Fournier M.J. The pseudouridine residues of ribosomal RNA: Number, location, biosynthesis, and function. In: Grosjean H., and Benne R. (Eds). "Modification and Editing of RNA: The Alteration of RNA Structure and Function" (1998), ASM Press, Washington, DC
    • (1998) "Modification and Editing of RNA: The Alteration of RNA Structure and Function"
    • Ofengand, J.1    Fournier, M.J.2
  • 102
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle J.M., Murphy F.V., Tarry M.J., and Ramakrishnan V. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111 (2002) 721-732
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 103
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle J.M., and Ramakrishnan V. Structural insights into translational fidelity. Annu. Rev. Biochem. 74 (2005) 129-177
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 105
    • 0037117533 scopus 로고    scopus 로고
    • In vitro reconstitution and activity of a C/D box methylation guide ribonucleoprotein complex
    • Omer A.D., Ziesche S., Ebhardt H., and Dennis P.P. In vitro reconstitution and activity of a C/D box methylation guide ribonucleoprotein complex. Proc. Natl. Acad. Sci. USA 99 (2002) 5289-5294
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5289-5294
    • Omer, A.D.1    Ziesche, S.2    Ebhardt, H.3    Dennis, P.P.4
  • 106
    • 0032489364 scopus 로고    scopus 로고
    • Temperature-sensitive mutations of the CKA1 gene reveal a role for casein kinase II in maintenance of cell polarity in Saccharomyces cerevisiae
    • Rethinaswamy A., Birnbaum M.J., and Glover C.V. Temperature-sensitive mutations of the CKA1 gene reveal a role for casein kinase II in maintenance of cell polarity in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 5869-5877
    • (1998) J. Biol. Chem. , vol.273 , pp. 5869-5877
    • Rethinaswamy, A.1    Birnbaum, M.J.2    Glover, C.V.3
  • 107
    • 0242414021 scopus 로고    scopus 로고
    • A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome
    • Robert F., and Brakier-Gingras L. A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome. J. Biol. Chem. 278 (2003) 44913-44920
    • (2003) J. Biol. Chem. , vol.278 , pp. 44913-44920
    • Robert, F.1    Brakier-Gingras, L.2
  • 108
    • 0037324527 scopus 로고    scopus 로고
    • Binding of L7Ae protein to the K-turn of archaeal snoRNAs: A shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea
    • Rozhdestvensky T., Tang T., Tchirkova I., Brosius J., Bachellerie J.-P., and Hüttenhofer A. Binding of L7Ae protein to the K-turn of archaeal snoRNAs: A shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea. Nucleic Acids Res. 31 (2003) 869-877
    • (2003) Nucleic Acids Res. , vol.31 , pp. 869-877
    • Rozhdestvensky, T.1    Tang, T.2    Tchirkova, I.3    Brosius, J.4    Bachellerie, J.-P.5    Hüttenhofer, A.6
  • 109
    • 4043120552 scopus 로고    scopus 로고
    • Genome-wide searching for pseudouridylation guide snoRNAs: Analysis of the Saccharomyces cerevisiae genome
    • Schattner P., Decatur W.A., Davis C.A., Ares Jr. M., Fournier M.J., and Lowe T.M. Genome-wide searching for pseudouridylation guide snoRNAs: Analysis of the Saccharomyces cerevisiae genome. Nucleic Acids Res. 32 (2004) 4281-4296
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4281-4296
    • Schattner, P.1    Decatur, W.A.2    Davis, C.A.3    Ares Jr., M.4    Fournier, M.J.5    Lowe, T.M.6
  • 110
    • 0024825036 scopus 로고
    • A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability
    • Schimmang T., Tollervey D., Kern H., Frank R., and Hurt E.C. A yeast nucleolar protein related to mammalian fibrillarin is associated with small nucleolar RNA and is essential for viability. EMBO J. 8 (1989) 4015-4024
    • (1989) EMBO J. , vol.8 , pp. 4015-4024
    • Schimmang, T.1    Tollervey, D.2    Kern, H.3    Frank, R.4    Hurt, E.C.5
  • 113
    • 45749130876 scopus 로고
    • Inhibition by antibiotics of the growth of bacterial and yeast protoplasts
    • Shockman G.D., and Lampen J.O. Inhibition by antibiotics of the growth of bacterial and yeast protoplasts. J. Bacteriol. 84 (1962) 508-512
    • (1962) J. Bacteriol. , vol.84 , pp. 508-512
    • Shockman, G.D.1    Lampen, J.O.2
  • 114
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., and Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122 (1989) 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 115
    • 0032745787 scopus 로고    scopus 로고
    • Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes
    • Sobel S.G., and Wolin S.L. Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes. Mol. Biol. Cell 10 (1999) 3849-3862
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3849-3862
    • Sobel, S.G.1    Wolin, S.L.2
  • 116
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions
    • Spahn C.M., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., and Frank J. Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions. Cell 107 (2001) 373-386
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 118
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence J., Gali R.R., Dittmar G., Sherman F., Karin M., and Finley D. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102 (2000) 67-76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 119
    • 0029070954 scopus 로고
    • Versatile vectors to study recoding: Conservation of rules between yeast and mammalian cells
    • Stahl G., Bidou L., Rousset J.P., and Cassan M. Versatile vectors to study recoding: Conservation of rules between yeast and mammalian cells. Nucleic Acids Res. 23 (1995) 1557-1560
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1557-1560
    • Stahl, G.1    Bidou, L.2    Rousset, J.P.3    Cassan, M.4
  • 120
    • 16544363622 scopus 로고    scopus 로고
    • Translational accuracy during exponential, postdiauxic, and stationary growth phases in Saccharomyces cerevisiae
    • Stahl G., Salem S.N., Chen L., Zhao B., and Farabaugh P.J. Translational accuracy during exponential, postdiauxic, and stationary growth phases in Saccharomyces cerevisiae. Eukaryot. Cell 3 (2004) 331-338
    • (2004) Eukaryot. Cell , vol.3 , pp. 331-338
    • Stahl, G.1    Salem, S.N.2    Chen, L.3    Zhao, B.4    Farabaugh, P.J.5
  • 121
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S., Moazed D., and Noller H.F. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol. 164 (1988) 481-489
    • (1988) Methods Enzymol. , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 122
    • 0033558377 scopus 로고    scopus 로고
    • A 2-mm DNA-based marker recycling system for multiple gene disruption in the yeast Saccharomyces cerevisiae
    • Storici F., Coglievina M., and Bruschi C.V. A 2-mm DNA-based marker recycling system for multiple gene disruption in the yeast Saccharomyces cerevisiae. Yeast 15 (1999) 271-283
    • (1999) Yeast , vol.15 , pp. 271-283
    • Storici, F.1    Coglievina, M.2    Bruschi, C.V.3
  • 123
    • 0344237362 scopus 로고    scopus 로고
    • Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3′ end of 18S rRNA
    • Tabb-Massey A., Caffrey J.M., Logsden P., Taylor S., Trent J.O., and Ellis S.R. Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have overlapping functions in the maturation of the 3′ end of 18S rRNA. Nucleic Acids Res. 31 (2003) 6798-6805
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6798-6805
    • Tabb-Massey, A.1    Caffrey, J.M.2    Logsden, P.3    Taylor, S.4    Trent, J.O.5    Ellis, S.R.6
  • 124
    • 0036743658 scopus 로고    scopus 로고
    • Uptake rate measurement of some amino acids on normal and treated yeast cells to xenobiotics using 14C labelled amino acid
    • Tanudjojo N., Soedigdo P., and Soedigdo S. Uptake rate measurement of some amino acids on normal and treated yeast cells to xenobiotics using 14C labelled amino acid. Food Nutr. Bull. 23 (2002) 61-65
    • (2002) Food Nutr. Bull. , vol.23 , pp. 61-65
    • Tanudjojo, N.1    Soedigdo, P.2    Soedigdo, S.3
  • 125
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
    • Tarun Jr. S.Z., Wells S.E., Deardorff J.A., and Sachs A.B. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94 (1997) 9046-9051
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9046-9051
    • Tarun Jr., S.Z.1    Wells, S.E.2    Deardorff, J.A.3    Sachs, A.B.4
  • 126
    • 33645465733 scopus 로고    scopus 로고
    • Antibiotics and the ribosome
    • Tenson T., and Mankin A. Antibiotics and the ribosome. Mol. Microbiol. 59 (2006) 1664-1677
    • (2006) Mol. Microbiol. , vol.59 , pp. 1664-1677
    • Tenson, T.1    Mankin, A.2
  • 127
    • 0024295811 scopus 로고
    • Sequence and genetic analysis of a dispensable 189 nucleotide snRNA from Saccharomyces cerevisiae
    • Thompson J.R., Zagorski J., Woolford J.L., and Fournier M.J. Sequence and genetic analysis of a dispensable 189 nucleotide snRNA from Saccharomyces cerevisiae. Nucleic Acids Res. 16 (1988) 5587-5601
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5587-5601
    • Thompson, J.R.1    Zagorski, J.2    Woolford, J.L.3    Fournier, M.J.4
  • 128
    • 0023661309 scopus 로고
    • A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA
    • Tollervey D. A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA. EMBO J. 6 (1987) 4169-4175
    • (1987) EMBO J. , vol.6 , pp. 4169-4175
    • Tollervey, D.1
  • 129
    • 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., and Hurt E.C. Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. Cell 72 (1993) 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
  • 130
    • 21844473540 scopus 로고    scopus 로고
    • The complete set of H/ACA snoRNAs that guide rRNA pseudouridylations in Saccharomyces cerevisiae
    • Torchet C., Badis G., Devaux F., Costanzo G., Werner M., and Jacquier A. The complete set of H/ACA snoRNAs that guide rRNA pseudouridylations in Saccharomyces cerevisiae. RNA 11 (2005) 928-938
    • (2005) RNA , vol.11 , pp. 928-938
    • Torchet, C.1    Badis, G.2    Devaux, F.3    Costanzo, G.4    Werner, M.5    Jacquier, A.6
  • 131
    • 0030479854 scopus 로고    scopus 로고
    • The red/white colony color assay in the yeast Saccharomyces cerevisiae: Epistatic growth advantage of white ade8-18, ade2 cells over red ade2 cells
    • Ugolini S., and Bruschi C.V. The red/white colony color assay in the yeast Saccharomyces cerevisiae: Epistatic growth advantage of white ade8-18, ade2 cells over red ade2 cells. Curr. Genet. 30 (1996) 485-492
    • (1996) Curr. Genet. , vol.30 , pp. 485-492
    • Ugolini, S.1    Bruschi, C.V.2
  • 132
    • 0034635334 scopus 로고    scopus 로고
    • Domain III of Saccharomyces cerevisiae 25 S ribosomal RNA: Its role in binding of ribosomal protein L25 and 60 S subunit formation
    • van Beekvelt C.A., Kooi E.A., de Graaff-Vincent M., Riet J., Venema J., and Raue H.A. Domain III of Saccharomyces cerevisiae 25 S ribosomal RNA: Its role in binding of ribosomal protein L25 and 60 S subunit formation. J. Mol. Biol. 296 (2000) 7-17
    • (2000) J. Mol. Biol. , vol.296 , pp. 7-17
    • van Beekvelt, C.A.1    Kooi, E.A.2    de Graaff-Vincent, M.3    Riet, J.4    Venema, J.5    Raue, H.A.6
  • 133
    • 0033862288 scopus 로고    scopus 로고
    • Mutations in helix 27 of the yeast Saccharomyces cerevisiae 18S rRNA affect the function of the decoding center of the ribosome
    • Velichutina I.V., Dresios J., Hong J.Y., Li C., Mankin A., Synetos D., and Liebman S.W. Mutations in helix 27 of the yeast Saccharomyces cerevisiae 18S rRNA affect the function of the decoding center of the ribosome. RNA 6 (2000) 1174-1184
    • (2000) RNA , vol.6 , pp. 1174-1184
    • Velichutina, I.V.1    Dresios, J.2    Hong, J.Y.3    Li, C.4    Mankin, A.5    Synetos, D.6    Liebman, S.W.7
  • 134
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema J., and Tollervey D. Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 33 (1999) 261-311
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 135
    • 0032246305 scopus 로고    scopus 로고
    • Identification and analysis of frameshift sites
    • Vimaladithan A., and Farabaugh P.J. Identification and analysis of frameshift sites. Methods Mol. Biol. 77 (1998) 399-411
    • (1998) Methods Mol. Biol. , vol.77 , pp. 399-411
    • Vimaladithan, A.1    Farabaugh, P.J.2
  • 136
    • 9344219606 scopus 로고    scopus 로고
    • Deletion of the three distal S1 motifs of Saccharomyces cerevisiae Rrp5p abolishes pre-rRNA processing at site A(2) without reducing the production of functional 40S subunits
    • Vos H.R., Faber A.W., de Gier M.D., Vos J.C., and Raue H.A. Deletion of the three distal S1 motifs of Saccharomyces cerevisiae Rrp5p abolishes pre-rRNA processing at site A(2) without reducing the production of functional 40S subunits. Eukaryot. Cell 3 (2004) 1504-1512
    • (2004) Eukaryot. Cell , vol.3 , pp. 1504-1512
    • Vos, H.R.1    Faber, A.W.2    de Gier, M.D.3    Vos, J.C.4    Raue, H.A.5
  • 137
    • 0034141555 scopus 로고    scopus 로고
    • Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution
    • Wang H., Boisvert D., Kim K.K., Kim R., and Kim S.H. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution. EMBO J. 19 (2000) 317-323
    • (2000) EMBO J. , vol.19 , pp. 317-323
    • Wang, H.1    Boisvert, D.2    Kim, K.K.3    Kim, R.4    Kim, S.H.5
  • 138
  • 139
    • 0029805781 scopus 로고    scopus 로고
    • Elements essential for processing intronic U14 snoRNA are located at the termini of the mature snoRNA sequence and include conserved nucleotide boxes C and D
    • Watkins N.J., Leverette R.D., Xia L., Andrews M.T., and Maxwell E.S. Elements essential for processing intronic U14 snoRNA are located at the termini of the mature snoRNA sequence and include conserved nucleotide boxes C and D. RNA 2 (1996) 118-133
    • (1996) RNA , vol.2 , pp. 118-133
    • Watkins, N.J.1    Leverette, R.D.2    Xia, L.3    Andrews, M.T.4    Maxwell, E.S.5
  • 140
    • 17644379370 scopus 로고    scopus 로고
    • Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits
    • West M., Hedges J.B., Chen A., and Johnson A.W. Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits. Mol. Cell Biol. 25 (2005) 3802-3813
    • (2005) Mol. Cell Biol. , vol.25 , pp. 3802-3813
    • West, M.1    Hedges, J.B.2    Chen, A.3    Johnson, A.W.4
  • 141
    • 13544262685 scopus 로고    scopus 로고
    • Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae
    • Williams I., Richardson J., Starkey A., and Stansfield I. Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae. Nucleic Acids Res. 32 (2004) 6605-6616
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6605-6616
    • Williams, I.1    Richardson, J.2    Starkey, A.3    Stansfield, I.4
  • 142
    • 0026030414 scopus 로고
    • Preparation and analysis of low molecular weight RNAs and small ribonucleoproteins
    • Wise J.A. Preparation and analysis of low molecular weight RNAs and small ribonucleoproteins. Methods Enzymol. 194 (1991) 405-415
    • (1991) Methods Enzymol. , vol.194 , pp. 405-415
    • Wise, J.A.1
  • 143
    • 33751009398 scopus 로고    scopus 로고
    • snoSeeker: An advanced computational package for screening of guide and orphan snoRNA genes in the human genome
    • Yang J.H., Zhang X.C., Huang Z.P., Zhou H., Huang M.B., Zhang S., Chen Y.Q., and Qu L.H. snoSeeker: An advanced computational package for screening of guide and orphan snoRNA genes in the human genome. Nucleic Acids Res. 34 (2006) 5112-5123
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5112-5123
    • Yang, J.H.1    Zhang, X.C.2    Huang, Z.P.3    Zhou, H.4    Huang, M.B.5    Zhang, S.6    Chen, Y.Q.7    Qu, L.H.8
  • 144
  • 146
    • 0035958587 scopus 로고    scopus 로고
    • The path of messenger RNA through the ribosome
    • Yusupova G.Z., Yusupov M.M., Cate J.H., and Noller H.F. The path of messenger RNA through the ribosome. Cell 106 (2001) 233-241
    • (2001) Cell , vol.106 , pp. 233-241
    • Yusupova, G.Z.1    Yusupov, M.M.2    Cate, J.H.3    Noller, H.F.4
  • 147
    • 15944384666 scopus 로고    scopus 로고
    • The expanding world of small RNAs in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Zago M.A., Dennis P.P., and Omer A.D. The expanding world of small RNAs in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol. 55 (2005) 1812-1828
    • (2005) Mol. Microbiol. , vol.55 , pp. 1812-1828
    • Zago, M.A.1    Dennis, P.P.2    Omer, A.D.3
  • 148
    • 0024062998 scopus 로고
    • Characterization of an SNR gene locus in Saccharomyces cerevisiae that specifies both dispensable and essential small nuclear RNAs
    • Zagorski J., Tollervey D., and Fournier M.J. Characterization of an SNR gene locus in Saccharomyces cerevisiae that specifies both dispensable and essential small nuclear RNAs. Mol. Cell Biol. 8 (1988) 3282-3290
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3282-3290
    • Zagorski, J.1    Tollervey, D.2    Fournier, M.J.3
  • 149
    • 0032718276 scopus 로고    scopus 로고
    • Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA
    • Zebarjadian Y., King T., Fournier M.J., Clarke L., and Carbon J. Point mutations in yeast CBF5 can abolish in vivo pseudouridylation of rRNA. Mol. Cell Biol. 19 (1999) 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
  • 150
    • 0027256768 scopus 로고
    • The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation
    • Zhong T., and Arndt K.T. The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73 (1993) 1175-1186
    • (1993) Cell , vol.73 , pp. 1175-1186
    • Zhong, T.1    Arndt, K.T.2


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