메뉴 건너뛰기




Volumn 20, Issue 10, 2014, Pages 1632-1644

A cluster of methylations in the domain IV of 25S rRNA is required for ribosome stability

Author keywords

Ribosomal RNA; Ribosome stability; RNA modification; Translation; Yeast

Indexed keywords

25S RIBOSOME RNA; DNA (CYTOSINE 5) METHYLTRANSFERASE; RIBONUCLEOPROTEIN; RIBOSE; RIBOSOME PROTEIN; RIBOSOME RNA; UNCLASSIFIED DRUG; FUNGAL RNA; METHYLTRANSFERASE; RNA, RIBOSOMAL, 25S; RPL23A PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL INTERFERING RNA;

EID: 84907198762     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.043398.113     Document Type: Article
Times cited : (63)

References (61)
  • 1
    • 0029687867 scopus 로고    scopus 로고
    • The importance of being modified: Roles of modified nucleosides and Mg2+ in RNA structure and function
    • Agris PF. 1996. The importance of being modified: roles of modified nucleosides and Mg2+ in RNA structure and function. Prog Nucleic Acid Res Mol Biol 53: 79-129.
    • (1996) Prog Nucleic Acid Res Mol Biol , vol.53 , pp. 79-129
    • Agris, P.F.1
  • 2
    • 78649301379 scopus 로고    scopus 로고
    • RiboSys, a high-resolution, quantitative approach to measure the in vivo kinetics of pre-mRNA splicing and 3'-end processing in Saccharomyces cerevisiae
    • Alexander RD, Barrass JD, Dichtl B, Kos M, Obtulowicz T, Robert M-C, Koper M, Karkusiewicz I, Mariconti L, Tollervey D, et al. 2010. RiboSys, a high-resolution, quantitative approach to measure the in vivo kinetics of pre-mRNA splicing and 3'-end processing in Saccharomyces cerevisiae. RNA 16: 2570-2580.
    • (2010) RNA , vol.16 , pp. 2570-2580
    • Alexander, R.D.1    Barrass, J.D.2    Dichtl, B.3    Kos, M.4    Obtulowicz, T.5    Robert, M.-C.6    Koper, M.7    Karkusiewicz, I.8    Mariconti, L.9    Tollervey, D.10
  • 4
    • 75649096366 scopus 로고    scopus 로고
    • Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy
    • Baudin-Baillieu A, Fabret C, Liang X-H, Piekna-Przybylska D, Fournier MJ, Rousset J-P. 2009. Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy. Nucleic Acids Res 37: 7665-7677.
    • (2009) Nucleic Acids Res , vol.37 , pp. 7665-7677
    • Baudin-Baillieu, A.1    Fabret, C.2    Liang, X.-H.3    Piekna-Przybylska, D.4    Fournier, M.J.5    Rousset, J.-P.6
  • 5
    • 34249868208 scopus 로고    scopus 로고
    • Optimization of ribosome structure and function by rRNA base modification
    • Baxter-Roshek JL, Petrov AN, Dinman JD. 2007. Optimization of ribosome structure and function by rRNA base modification. PLoS One 2: e174.
    • (2007) PLoS One , vol.2
    • Baxter-Roshek, J.L.1    Petrov, A.N.2    Dinman, J.D.3
  • 6
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem A, Jenner L, Yusupova G, Yusupov M. 2010. Crystal structure of the eukaryotic ribosome. Science 330: 1203-1209.
    • (2010) Science , vol.330 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 8
    • 2342643512 scopus 로고    scopus 로고
    • Sequence-structure- function studies of tRNA:m5C methyltransferase Trm4p and its relationship to DNA:m5C and RNA:m5U methyltransferases
    • Bujnicki JM, Feder M, Ayres CL, Redman KL. 2004. Sequence-structure- function studies of tRNA:m5C methyltransferase Trm4p and its relationship to DNA:m5C and RNA:m5U methyltransferases. Nucleic Acids Res 32: 2453-2463.
    • (2004) Nucleic Acids Res , vol.32 , pp. 2453-2463
    • Bujnicki, J.M.1    Feder, M.2    Ayres, C.L.3    Redman, K.L.4
  • 9
    • 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
  • 10
    • 35648960799 scopus 로고    scopus 로고
    • Expanding the nucleotide repertoire of the ribosome with post-transcriptional modifications
    • Chow CS, Lamichhane TN, Mahto SK. 2007. Expanding the nucleotide repertoire of the ribosome with post-transcriptional modifications. ACS Chem Biol 2: 610-619.
    • (2007) ACS Chem Biol , vol.2 , pp. 610-619
    • Chow, C.S.1    Lamichhane, T.N.2    Mahto, S.K.3
  • 11
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox J, Matic I, Hilger M, Nagaraj N, Selbach M, Olsen JV, Mann M. 2009. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat Protoc 4: 698-705.
    • (2009) Nat Protoc , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 12
    • 0029566314 scopus 로고
    • Stabilization of RNA stacking by pseudouridine
    • Davis DR. 1995. Stabilization of RNA stacking by pseudouridine. Nucleic Acids Res 23: 5020-5026.
    • (1995) Nucleic Acids Res , vol.23 , pp. 5020-5026
    • Davis, D.R.1
  • 13
    • 0002841715 scopus 로고    scopus 로고
    • Biophysical and conformational properties of modified nucleosides in RNA (nuclear magnetic resonance studies)
    • (ed. Grosjean H, Benne R), ASM Press, Washington, DC
    • Davis DR. 1998. Biophysical and conformational properties of modified nucleosides in RNA (nuclear magnetic resonance studies). In Modification and editing of RNA (ed. Grosjean H, Benne R), pp. 85-102. ASM Press, Washington, DC.
    • (1998) Modification and Editing of RNA , pp. 85-102
    • Davis, D.R.1
  • 14
    • 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
  • 15
    • 34548751838 scopus 로고    scopus 로고
    • Identifying effects of snoRNA-guided modifications on the synthesis and function of the yeast ribosome
    • Decatur WA, Liang X, Piekna-Przybylska D, Fournier MJ. 2007. Identifying effects of snoRNA-guided modifications on the synthesis and function of the yeast ribosome. Methods Enzymol 425: 283-316.
    • (2007) Methods Enzymol , vol.425 , pp. 283-316
    • Decatur, W.A.1    Liang, X.2    Piekna-Przybylska, D.3    Fournier, M.J.4
  • 16
    • 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
  • 17
    • 0030966221 scopus 로고    scopus 로고
    • Peptidyl-transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: Development of model systems
    • Dinman JD, Ruiz-Echevarria MJ, Czaplinski K, Peltz SW. 1997. Peptidyl-transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: development of model systems. Proc Natl Acad Sci 94: 6606-6611.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 6606-6611
    • Dinman, J.D.1    Ruiz-Echevarria, M.J.2    Czaplinski, K.3    Peltz, S.W.4
  • 18
    • 0032054710 scopus 로고    scopus 로고
    • Translating old drugs into new treatments: Ribosomal frameshifting as a target for antiviral agents
    • Dinman JD, Ruiz-Echevarria MJ, Peltz SW. 1998. Translating old drugs into new treatments: ribosomal frameshifting as a target for antiviral agents. Trends Biotechnol 16: 190-196.
    • (1998) Trends Biotechnol , vol.16 , pp. 190-196
    • Dinman, J.D.1    Ruiz-Echevarria, M.J.2    Peltz, S.W.3
  • 19
    • 0014945408 scopus 로고
    • Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits
    • Falvey AK, Staehelin T. 1970. Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits. J Mol Biol 53: 1-19.
    • (1970) J Mol Biol , vol.53 , pp. 1-19
    • Falvey, A.K.1    Staehelin, T.2
  • 20
    • 0032571359 scopus 로고    scopus 로고
    • Paromomycin binding induces a local conformational change in the A-site of 16 s rRNA
    • Fourmy D, Yoshizawa S, Puglisi JD. 1998. Paromomycin binding induces a local conformational change in the A-site of 16 s rRNA. J Mol Biol 277: 333-345.
    • (1998) J Mol Biol , vol.277 , pp. 333-345
    • Fourmy, D.1    Yoshizawa, S.2    Puglisi, J.D.3
  • 22
    • 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
  • 24
    • 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
  • 26
    • 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
  • 27
    • 0035878934 scopus 로고    scopus 로고
    • Temperature sensitive nop2 alleles defective in synthesis of 25S rRNA and large ribosomal subunits in Saccharomyces cerevisiae
    • Hong B, Wu K, Brockenbrough JS, Wu P, Aris JP. 2001. Temperature sensitive nop2 alleles defective in synthesis of 25S rRNA and large ribosomal subunits in Saccharomyces cerevisiae. Nucleic Acids Res 29: 2927-2937.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2927-2937
    • Hong, B.1    Wu, K.2    Brockenbrough, J.S.3    Wu, P.4    Aris, J.P.5
  • 28
    • 0015102782 scopus 로고
    • Pressure-induced dissociation of sedimenting ribosomes: Effect on sedimentation patterns
    • Infante AA, Baierlein R. 1971. Pressure-induced dissociation of sedimenting ribosomes: effect on sedimentation patterns. Proc Natl Acad Sci 68: 1780-1785.
    • (1971) Proc Natl Acad Sci , vol.68 , pp. 1780-1785
    • Infante, A.A.1    Baierlein, R.2
  • 30
    • 0037125961 scopus 로고    scopus 로고
    • RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine
    • King MY, Redman KL. 2002. RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine. Biochemistry 41: 11218-11225.
    • (2002) Biochemistry , vol.41 , pp. 11218-11225
    • King, M.Y.1    Redman, K.L.2
  • 31
    • 0032959714 scopus 로고    scopus 로고
    • A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue
    • King M, Ton D, Redman KL. 1999. A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue. Biochem J 337: 29-35.
    • (1999) Biochem J , vol.337 , pp. 29-35
    • King, M.1    Ton, D.2    Redman, K.L.3
  • 33
    • 80053081195 scopus 로고    scopus 로고
    • Mass spectrometric-based quantitative proteomics using SILAC
    • (ed. Jameson D, et al.), Elsevier, Amsterdam, Netherlands
    • Lanucara F, Eyers CE. 2011. Mass spectrometric-based quantitative proteomics using SILAC. In Methods in enzymology (ed. Jameson D, et al.), Vol. 500, pp. 133-150. Elsevier, Amsterdam, Netherlands.
    • (2011) Methods in Enzymology , vol.500 , pp. 133-150
    • Lanucara, F.1    Eyers, C.E.2
  • 34
    • 0029074526 scopus 로고
    • Role for the highly conserved region of domain IV of 23S-like rRNA in subunit-subunit interactions at the peptidyl transferase centre
    • Leviev I, Levieva S, Garrett RA. 1995. Role for the highly conserved region of domain IV of 23S-like rRNA in subunit-subunit interactions at the peptidyl transferase centre. Nucleic Acids Res 23: 1512-1517.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1512-1517
    • Leviev, I.1    Levieva, S.2    Garrett, R.A.3
  • 35
    • 37349128219 scopus 로고    scopus 로고
    • RRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity
    • Liang X, Liu Q, Fournier MJ. 2007. rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity. Mol Cell 28: 965-977.
    • (2007) Mol Cell , vol.28 , pp. 965-977
    • Liang, X.1    Liu, Q.2    Fournier, M.J.3
  • 36
    • 69049089806 scopus 로고    scopus 로고
    • Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing
    • Liang X, Liu Q, Fournier MJ. 2009. Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing. RNA 15: 1716-1728.
    • (2009) RNA , vol.15 , pp. 1716-1728
    • Liang, X.1    Liu, Q.2    Fournier, M.J.3
  • 37
  • 38
    • 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
  • 39
    • 0014961540 scopus 로고
    • Resistance of active yeast ribosomes to dissociation by KCl
    • Martin TE, Hartwell LH. 1970. Resistance of active yeast ribosomes to dissociation by KCl. J Biol Chem 245: 1504-1506.
    • (1970) J Biol Chem , vol.245 , pp. 1504-1506
    • Martin, T.E.1    Hartwell, L.H.2
  • 40
    • 79952591194 scopus 로고    scopus 로고
    • Polysome analysis and RNA purification from sucrose gradients
    • Mašek T, Valášek L, Pospíšek M. 2011. Polysome analysis and RNA purification from sucrose gradients. Methods Mol Biol 703: 293-309.
    • (2011) Methods Mol Biol , vol.703 , pp. 293-309
    • Mašek, T.1    Valášek, L.2    Pospíšek, M.3
  • 41
    • 85011940405 scopus 로고    scopus 로고
    • The "fifth" RNA nucleotide: A role for ribosomal RNA pseudouridylation in control of gene expression at the translational level
    • (ed. Dinman JD), Biophysics for the Life Sciences, Springer, New York
    • McMahon M, Bellodi C, Ruggero D. 2013. The "fifth" RNA nucleotide: a role for ribosomal RNA pseudouridylation in control of gene expression at the translational level. In Biophysical approaches to translational control of gene expression (ed. Dinman JD), pp. 253-288. Biophysics for the Life Sciences, Springer, New York.
    • (2013) Biophysical Approaches to Translational Control of Gene Expression , pp. 253-288
    • McMahon, M.1    Bellodi, C.2    Ruggero, D.3
  • 42
    • 34247162792 scopus 로고    scopus 로고
    • A fast-acting reagent for accurate analysis of RNA secondary and tertiary structure by SHAPE chemistry
    • Mortimer SA, Weeks KM. 2007. A fast-acting reagent for accurate analysis of RNA secondary and tertiary structure by SHAPE chemistry. J Am Chem Soc 129: 4144-4145.
    • (2007) J Am Chem Soc , vol.129 , pp. 4144-4145
    • Mortimer, S.A.1    Weeks, K.M.2
  • 43
    • 24644437810 scopus 로고    scopus 로고
    • RNA structure: Reading the ribosome
    • Noller HF. 2005. RNA structure: reading the ribosome. Science 309: 1508-1514.
    • (2005) Science , vol.309 , pp. 1508-1514
    • Noller, H.F.1
  • 44
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S-E, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 45
    • 70449498766 scopus 로고    scopus 로고
    • Multiple Motif Scanning to identify methyltransferases from the yeast proteome
    • Petrossian TC, Clarke SG. 2009. Multiple Motif Scanning to identify methyltransferases from the yeast proteome. Mol Cell Proteomics 8: 1516-1526.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1516-1526
    • Petrossian, T.C.1    Clarke, S.G.2
  • 46
    • 33847270751 scopus 로고    scopus 로고
    • New bioinformatic tools for analysis of nucleotide modifications in eukaryotic rRNA
    • Piekna-Przybylska D, Decatur WA, Fournier MJ. 2007. New bioinformatic tools for analysis of nucleotide modifications in eukaryotic rRNA. RNA 13: 305-312.
    • (2007) RNA , vol.13 , pp. 305-312
    • Piekna-Przybylska, D.1    Decatur, W.A.2    Fournier, M.J.3
  • 47
    • 54449100396 scopus 로고    scopus 로고
    • Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit
    • Piekna-Przybylska D, Przybylski P, Baudin-Baillieu A, Rousset J-P, Fournier MJ. 2008. Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit. J Biol Chem 283: 26026-26036.
    • (2008) J Biol Chem , vol.283 , pp. 26026-26036
    • Piekna-Przybylska, D.1    Przybylski, P.2    Baudin-Baillieu, A.3    Rousset, J.-P.4    Fournier, M.J.5
  • 48
    • 79956268777 scopus 로고    scopus 로고
    • An extensive network of information flow through the B1b/c intersubunit bridge of the yeast ribosome
    • Rhodin MHJ, Dinman JD. 2011. An extensive network of information flow through the B1b/c intersubunit bridge of the yeast ribosome. PLoS One 6: e20048.
    • (2011) PLoS One , vol.6
    • Rhodin, M.H.J.1    Dinman, J.D.2
  • 50
    • 84885993080 scopus 로고    scopus 로고
    • Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively
    • Sharma S, Yang J, Watzinger P, Kötter P, Entian K-D. 2013. Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively. Nucleic Acids Res 41: 9062-9076.
    • (2013) Nucleic Acids Res , vol.41 , pp. 9062-9076
    • Sharma, S.1    Yang, J.2    Watzinger, P.3    Kötter, P.4    Entian, K.-D.5
  • 51
    • 0029070954 scopus 로고
    • Versatile vectors to study recoding: Conservation of rules between yeast and mammalian cells
    • Stahl G, Bidou L, Rousset J-P, Cassan M. 1995. Versatile vectors to study recoding: conservation of rules between yeast and mammalian cells. Nucleic Acids Res 23: 1557-1560.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1557-1560
    • Stahl, G.1    Bidou, L.2    Rousset, J.-P.3    Cassan, M.4
  • 52
    • 0023286894 scopus 로고
    • Fungal small nuclear ribonucleoproteins share properties with plant and vertebrate U-snRNPs
    • Tollervey D, Mattaj IW. 1987. Fungal small nuclear ribonucleoproteins share properties with plant and vertebrate U-snRNPs. EMBO J 6: 469-476.
    • (1987) EMBO J , vol.6 , pp. 469-476
    • Tollervey, D.1    Mattaj, I.W.2
  • 53
    • 0025963863 scopus 로고
    • The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast
    • Tollervey D, Lehtonen H, Carmo-Fonseca M, Hurt EC. 1991. The small nucleolar RNP protein NOP1 (fibrillarin) is required for pre-rRNA processing in yeast. EMBO J 10: 573-583.
    • (1991) EMBO J , vol.10 , pp. 573-583
    • Tollervey, D.1    Lehtonen, H.2    Carmo-Fonseca, M.3    Hurt, E.C.4
  • 54
    • 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
  • 55
    • 27744435957 scopus 로고    scopus 로고
    • Additional vectors for PCR-based gene tagging in Saccharomyces cerevisiae and Schizosaccharomyces pombe using nourseothricin resistance
    • Van Driessche B, Tafforeau L, Hentges P, Carr AM, Vandenhaute J. 2005. Additional vectors for PCR-based gene tagging in Saccharomyces cerevisiae and Schizosaccharomyces pombe using nourseothricin resistance. Yeast 22: 1061-1068.
    • (2005) Yeast , vol.22 , pp. 1061-1068
    • Van Driessche, B.1    Tafforeau, L.2    Hentges, P.3    Carr, A.M.4    Vandenhaute, J.5
  • 56
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach A, Brachat A, Pöhlmann R, Philippsen P. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10: 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 57
    • 33645744221 scopus 로고    scopus 로고
    • The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains over 200 genes
    • Wade CH, Umbarger MA, McAlear MA. 2006. The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains over 200 genes. Yeast 23: 293-306.
    • (2006) Yeast , vol.23 , pp. 293-306
    • Wade, C.H.1    Umbarger, M.A.2    McAlear, M.A.3
  • 58
    • 33947720028 scopus 로고    scopus 로고
    • Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • Wilkinson KA, Merino EJ, Weeks KM. 2006. Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution. Nat Protoc 1: 1610-1616.
    • (2006) Nat Protoc , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 60
    • 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
  • 61
    • 0014954681 scopus 로고
    • The effect of high ionic strength on monomers, polyribosomes, and puromycin-treated polyribosomes
    • Zylber EA, Penman S. 1970. The effect of high ionic strength on monomers, polyribosomes, and puromycin-treated polyribosomes. Biochim Biophys Acta 204: 221-229.
    • (1970) Biochim Biophys Acta , vol.204 , pp. 221-229
    • Zylber, E.A.1    Penman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.