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Volumn 36, Issue 5, 2008, Pages 1497-1507

rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance

Author keywords

[No Author keywords available]

Indexed keywords

ANISOMYCIN; ANTIFUNGAL AGENT; ENZYME INHIBITOR; PAROMOMYCIN; PEPTIDYLTRANSFERASE; RIBOSOME RNA; SPARSOMYCIN; TRANSFER RNA;

EID: 41149135521     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm1179     Document Type: Article
Times cited : (33)

References (69)
  • 1
    • 36348996412 scopus 로고    scopus 로고
    • Origins and principles of translational control
    • Mathews,M.B, Sonenberg,N. and Hershey,J.W.B, eds, Cold Spring Harbor Press, Cold Spring Harbor, NY, pp
    • Mathews,M.B., Sonenberg,N. and Hershey,J.W.B. (2007) Origins and principles of translational control. In Mathews,M.B., Sonenberg,N. and Hershey,J.W.B. (eds), Translational Control in Biology and Medicine Cold Spring Harbor Press, Cold Spring Harbor, NY, pp. 1-40.
    • (2007) Translational Control in Biology and Medicine , pp. 1-40
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.B.3
  • 2
    • 0030970289 scopus 로고    scopus 로고
    • Ribosomes and translation
    • Green,R. and Noller,H.F. (1997) Ribosomes and translation. Annu. Rev. Biochem., 66, 679-716.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 679-716
    • Green, R.1    Noller, H.F.2
  • 4
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4Å resolution
    • Ban,N., Nissen,P., Hansen,J., Moore,P.B. and Steitz,T.A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4Å 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
  • 7
    • 27644502679 scopus 로고    scopus 로고
    • Simulating movement of tRNA into the ribosome during decoding
    • Sanbonmatsu,K.Y., Joseph,S. and Tung,C.S. (2005) Simulating movement of tRNA into the ribosome during decoding. Proc. Natl Acad. Sci. USA, 102, 15854-15859.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15854-15859
    • Sanbonmatsu, K.Y.1    Joseph, S.2    Tung, C.S.3
  • 8
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyi-tRNA
    • Schmeing,T.M., Huang,K.S., Strobel,S.A. and Steitz,T.A. (2005) An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyi-tRNA. Nature, 438, 520-524.
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 10
    • 34447302886 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
    • Unbehaun,A., Marintchev,A., Lomakin,I.B., Didenko,T., Wagner,G., Hellen,C.U. and Pestova,T.V. (2007) Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing. EMBO J., 26, 3109-3123.
    • (2007) EMBO J , vol.26 , pp. 3109-3123
    • Unbehaun, A.1    Marintchev, A.2    Lomakin, I.B.3    Didenko, T.4    Wagner, G.5    Hellen, C.U.6    Pestova, T.V.7
  • 11
    • 33747886005 scopus 로고    scopus 로고
    • The ribosome's response to codon-anticodon mismatches
    • Daviter,T., Gromadski,K.B. and Rodnina,M.V. (2006) The ribosome's response to codon-anticodon mismatches. Biochimie, 88, 1001-1011.
    • (2006) Biochimie , vol.88 , pp. 1001-1011
    • Daviter, T.1    Gromadski, K.B.2    Rodnina, M.V.3
  • 12
    • 18844408328 scopus 로고    scopus 로고
    • An active role for tRNA in decoding beyond codon:aNticodon pairing
    • Cochella,L. and Green,R. (2005) An active role for tRNA in decoding beyond codon:aNticodon pairing. Science, 308, 1178-1180.
    • (2005) Science , vol.308 , pp. 1178-1180
    • Cochella, L.1    Green, R.2
  • 13
    • 24744468042 scopus 로고    scopus 로고
    • Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G
    • Sergiev,P.V., Lesnyak,D.V., Burakovsky,D.E., Kiparisov,S.V., Leonov,A.A., Bogdanov,A.A., Brimacombe,R. and Dontsova,O.A. (2005) Alteration in location of a conserved GTPase-associated center of the ribosome induced by mutagenesis influences the structure of peptidyltransferase center and activity of elongation factor G. J. Biol. Chem., 280, 31882-31889.
    • (2005) J. Biol. Chem , vol.280 , pp. 31882-31889
    • Sergiev, P.V.1    Lesnyak, D.V.2    Burakovsky, D.E.3    Kiparisov, S.V.4    Leonov, A.A.5    Bogdanov, A.A.6    Brimacombe, R.7    Dontsova, O.A.8
  • 14
    • 41149155904 scopus 로고    scopus 로고
    • 5S rRNA: Structure and function from head to toe
    • Dontsova,O.A. and Dinman,J.D. (2005) 5S rRNA: Structure and function from head to toe. Int. J. Biomed. Sci., 1, 2-7.
    • (2005) Int. J. Biomed. Sci , vol.1 , pp. 2-7
    • Dontsova, O.A.1    Dinman, J.D.2
  • 15
    • 33845228894 scopus 로고    scopus 로고
    • An arc of unpaired "hinge bases" facilitates information exchange among functional centers of the ribosome
    • Rakauskaite,R. and Dinman,J.D. (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
  • 18
    • 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. (2004) Isolation of antibiotic resistance mutations in the rRNA by using an in vitro selection system. Proc. Natl Acad. Sci. USA, 101, 3786-3791.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3786-3791
    • Cochella, L.1    Green, R.2
  • 19
    • 0031566952 scopus 로고    scopus 로고
    • Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome
    • Green,R., Samaha,R.R. and Noller,H.F. (1997) Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome. J. Mol. Biol., 266, 40-50.
    • (1997) J. Mol. Biol , vol.266 , pp. 40-50
    • Green, R.1    Samaha, R.R.2    Noller, H.F.3
  • 20
    • 23044457405 scopus 로고    scopus 로고
    • Affinity purification of in vivo-assembled ribosomes for in vitro biochemical analysis
    • Youngman,E.M. and Green,R. (2005) Affinity purification of in vivo-assembled ribosomes for in vitro biochemical analysis. Methods 36, 305-312.
    • (2005) Methods , vol.36 , pp. 305-312
    • Youngman, E.M.1    Green, R.2
  • 21
    • 0037245660 scopus 로고    scopus 로고
    • The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination
    • Polacek,N., Gomez,M.J., Ito,K., Xiong,L.Q., Nakamura,Y. and Mankin,A. (2003) The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination. Mol. Cell, 11, 103-112.
    • (2003) Mol. Cell , vol.11 , pp. 103-112
    • Polacek, N.1    Gomez, M.J.2    Ito, K.3    Xiong, L.Q.4    Nakamura, Y.5    Mankin, A.6
  • 22
    • 33645462490 scopus 로고    scopus 로고
    • Efficient ribosomal peptidyl transfer critically relies on the presence of the ribose 2′-OH at A2451 of 23S rRNA
    • Erlacher,M.D., Lang,K., Wotzel,B., Rieder,R., Micura,R. and Polacek,N. (2006) Efficient ribosomal peptidyl transfer critically relies on the presence of the ribose 2′-OH at A2451 of 23S rRNA. J. Am. Chem. Soc., 128, 4453-4459.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4453-4459
    • Erlacher, M.D.1    Lang, K.2    Wotzel, B.3    Rieder, R.4    Micura, R.5    Polacek, N.6
  • 23
    • 17844367581 scopus 로고    scopus 로고
    • Nonbridging phosphate oxygens 16S rRNA important for 30S subunit assembly and association with the 50S ribosomal subunit
    • Ghosh,S. and Joseph,S. (2005) Nonbridging phosphate oxygens 16S rRNA important for 30S subunit assembly and association with the 50S ribosomal subunit. RNA, 11, 657-667.
    • (2005) RNA , vol.11 , pp. 657-667
    • Ghosh, S.1    Joseph, S.2
  • 24
    • 0033515041 scopus 로고    scopus 로고
    • An Escherichia coli strain with all chromosomal rRNA operons inactivated: Complete exchange of rRNA genes between bacteria
    • Asai,T., Zaporojets,D., Squires,C. and Squires,C.L. (1999) An Escherichia coli strain with all chromosomal rRNA operons inactivated: Complete exchange of rRNA genes between bacteria. Proc. Natl Acad. Sci. USA, 96, 1971-1976.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1971-1976
    • Asai, T.1    Zaporojets, D.2    Squires, C.3    Squires, C.L.4
  • 25
    • 0032487530 scopus 로고    scopus 로고
    • Mutational analysis of the structure and localization of the nucleolus in the yeast Saccharomyces cerevisiae
    • Oakes,M., Aris,J.P., Brockenbrough,J.S., Wai,H., Vu,L. and Nomura,M. (1998) Mutational analysis of the structure and localization of the nucleolus in the yeast Saccharomyces cerevisiae. J. Cell Biol., 143, 23-34.
    • (1998) J. Cell Biol , vol.143 , pp. 23-34
    • Oakes, M.1    Aris, J.P.2    Brockenbrough, J.S.3    Wai, H.4    Vu, L.5    Nomura, M.6
  • 26
    • 0034666440 scopus 로고    scopus 로고
    • Complete deletion of yeast chromosomal rDNA repeats and integration of a new rDNA repeat: Use of rDNA deletion strains for functional analysis of rDNA promoter elements in vivo
    • Wai,H.H., Vu,L., Oakes,M. and Nomura,M. (2000) Complete deletion of yeast chromosomal rDNA repeats and integration of a new rDNA repeat: Use of rDNA deletion strains for functional analysis of rDNA promoter elements in vivo. Nucleic Acids Res., 28, 3524-3534.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3524-3534
    • Wai, H.H.1    Vu, L.2    Oakes, M.3    Nomura, M.4
  • 27
    • 0017295312 scopus 로고
    • Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae
    • Wickner,R.B. and Leibowitz,M.J. (1976) Two chromosomal genes required for killing expression in killer strains of Saccharomyces cerevisiae. Genetics, 82, 429-442.
    • (1976) Genetics , vol.82 , pp. 429-442
    • Wickner, R.B.1    Leibowitz, M.J.2
  • 29
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito,H., Fukuda,Y., Murata,K. and 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
  • 30
    • 7044260452 scopus 로고    scopus 로고
    • Evidence against a direct role for the Upf proteins in frameshifting or nonsense codon readthrough
    • Harger,J.W. and Dinman,J.D. (2004) Evidence against a direct role for the Upf proteins in frameshifting or nonsense codon readthrough. RNA 10, 1721-1729.
    • (2004) RNA , vol.10 , pp. 1721-1729
    • Harger, J.W.1    Dinman, J.D.2
  • 31
    • 16544392668 scopus 로고    scopus 로고
    • Systematic analysis of bicistronic reporter assay data
    • Jacobs,J.L. and Dinman,J.D. (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
  • 32
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • Jung,G. and Masison,D.C. (2001) Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions. Curr. Microbiol., 43, 7-10.
    • (2001) Curr. Microbiol , vol.43 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 33
    • 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. (2005) Identification of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis. Mol. Cell Biol., 25, 10863-10874.
    • (2005) Mol. Cell Biol , vol.25 , pp. 10863-10874
    • Meskauskas, A.1    Petrov, A.N.2    Dinman, J.D.3
  • 34
    • 0024416021 scopus 로고
    • The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation
    • Sachs,A.B. and Davis,R.W. (1989) The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell, 58, 857-867.
    • (1989) Cell , vol.58 , pp. 857-867
    • Sachs, A.B.1    Davis, R.W.2
  • 35
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern,S., Moazed,D. and Noller,H.F. (1988) Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol., 164, 481-489.
    • (1988) Methods Enzymol , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 36
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen,J.L., Moore,P.B. and Steitz,T.A. (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
  • 37
    • 33751316103 scopus 로고    scopus 로고
    • A late-acting quality control process for mature eukaryotic rRNAs
    • LaRiviere,F.J., Cole,S.E., Ferullo,D.J. and Moore,M.J. (2006) A late-acting quality control process for mature eukaryotic rRNAs. Mol. Cell, 24, 619-626.
    • (2006) Mol. Cell , vol.24 , pp. 619-626
    • LaRiviere, F.J.1    Cole, S.E.2    Ferullo, D.J.3    Moore, M.J.4
  • 38
    • 0025873734 scopus 로고
    • An approach for isolation of mutants defective in 35S ribosomal RNA synthesis in Saccharomyces cerevisiae
    • Nogi,Y., Vu,L. and Nomura,M. (1991) An approach for isolation of mutants defective in 35S ribosomal RNA synthesis in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 88, 7026-7030.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7026-7030
    • Nogi, Y.1    Vu, L.2    Nomura, M.3
  • 39
    • 0035881963 scopus 로고    scopus 로고
    • Transcription of chromosomal rRNA genes by both RNA polymerase I and II in yeast uaf30 mutants lacking the 30kDa subunit of transcription factor UAF
    • Siddiqi,I.N., Dodd,J.A., Vu,L., Eliason,K., Oakes,M.L., Keener,J., Moore,R., Young,M.K. and Nomura,M. (2001) Transcription of chromosomal rRNA genes by both RNA polymerase I and II in yeast uaf30 mutants lacking the 30kDa subunit of transcription factor UAF. EMBO J., 20, 4512-4521.
    • (2001) EMBO J , vol.20 , pp. 4512-4521
    • Siddiqi, I.N.1    Dodd, J.A.2    Vu, L.3    Eliason, K.4    Oakes, M.L.5    Keener, J.6    Moore, R.7    Young, M.K.8    Nomura, M.9
  • 42
    • 0014198715 scopus 로고
    • Inhibitors of protein biosynthesis. II. Mode of action of anisomycin
    • Grollman,A.P. (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
  • 43
    • 0022409013 scopus 로고
    • Intermolecular exon ligation of the rRNA precursor of Tetrahymena: Oligonucleotides can function as 5′ exons
    • Inoue,T., Sullivan,F.X. and Cech,T.R. (1985) Intermolecular exon ligation of the rRNA precursor of Tetrahymena: Oligonucleotides can function as 5′ exons. Cell, 43, 431-437.
    • (1985) Cell , vol.43 , pp. 431-437
    • Inoue, T.1    Sullivan, F.X.2    Cech, T.R.3
  • 44
    • 0032831634 scopus 로고    scopus 로고
    • Relationship between internucleotide linkage geometry and the stability of RNA
    • Soukup,G.A. and Breaker,R.R. (1999) Relationship between internucleotide linkage geometry and the stability of RNA. RNA, 5, 1308-1325.
    • (1999) RNA , vol.5 , pp. 1308-1325
    • Soukup, G.A.1    Breaker, R.R.2
  • 45
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca,C., Amils,R. and Garrett,R.A. (1995) Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J. Mol. Biol., 247 224-235.
    • (1995) J. Mol. Biol , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 46
    • 0015195582 scopus 로고
    • Inhibitors of ribosome functions
    • Pestka,S. (1971) Inhibitors of ribosome functions. Annu. Rev. Microbiol., 25, 487-562.
    • (1971) Annu. Rev. Microbiol , vol.25 , pp. 487-562
    • Pestka, S.1
  • 47
    • 34249868208 scopus 로고    scopus 로고
    • Optimization of ribosome structure and function by rRNA base modification
    • Baxter-Roshek,J.L., Petrov,A.N. and Dinman,J.D. (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
  • 48
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter,A.P., Clemons,W.M., Brodersen,D.E., Morgan-Warren,R.J., Wimberly,B.T. and Ramakrishnan,V. (2000) Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature, 407, 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 49
    • 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. (2000) Yeast ribosomal protein L24 affects the kinetics of protein synthesis and ribosomal protein L39 improves translational accuracy, while mutants lacking both remain viable. Biochemistry, 39, 7236-7244.
    • (2000) Biochemistry , vol.39 , pp. 7236-7244
    • Dresios, J.1    Derkatch, I.L.2    Liebman, S.W.3    Synetos, D.4
  • 51
    • 0026031180 scopus 로고
    • A mutation in the large subunit ribosomal RNA gene of Tetrahymena confers anisomycin resistance and cold sensitivity
    • Sweeney,R., Yao,C.H. and Yao,M.C. (1991) A mutation in the large subunit ribosomal RNA gene of Tetrahymena confers anisomycin resistance and cold sensitivity. Genetics, 127, 327-334.
    • (1991) Genetics , vol.127 , pp. 327-334
    • Sweeney, R.1    Yao, C.H.2    Yao, M.C.3
  • 52
    • 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. (2003) Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center. Mol. Cell, 11, 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
  • 53
    • 0018379922 scopus 로고
    • Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics
    • Palmer,E., Wilhelm,J. and Sherman,F. (1979) Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics. Nature, 277, 148-150.
    • (1979) Nature , vol.277 , pp. 148-150
    • Palmer, E.1    Wilhelm, J.2    Sherman, F.3
  • 54
    • 0042703890 scopus 로고    scopus 로고
    • An in vivo dual-luciferase assay system for studying translational recoding in the yeast Saccharomyces cerevisiae
    • Harger,J.W. and Dinman,J.D. (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
  • 55
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner,R.B. (1994) [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae. Science, 264, 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 56
    • 29844448116 scopus 로고    scopus 로고
    • The interaction between C75 of tRNA and the A loop of the ribosome stimulates peptidyl transferase activity
    • Brunelle,J.L., Youngman,E.M., Sharma,D. and Green,R. (2006) The interaction between C75 of tRNA and the A loop of the ribosome stimulates peptidyl transferase activity. RNA, 12, 33-39.
    • (2006) RNA , vol.12 , pp. 33-39
    • Brunelle, J.L.1    Youngman, E.M.2    Sharma, D.3    Green, R.4
  • 57
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome
    • Samaha,R.R., Green,R. and Noller,H.F. (1995) A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome. Nature, 377, 309-314.
    • (1995) Nature , vol.377 , pp. 309-314
    • Samaha, R.R.1    Green, R.2    Noller, H.F.3
  • 59
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman,E.M., Brunelle,J.L., Kochaniak,A.B. and Green,R. (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117, 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 60
    • 0013869496 scopus 로고
    • Reconstitution of functionally active ribosomes from inactive subparticles and proteins
    • Hosokawa,K., Fujimura,R.K. and Nomura,M. (1966) Reconstitution of functionally active ribosomes from inactive subparticles and proteins. Proc. Natl Acad. Sci. USA, 55, 198-204.
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , pp. 198-204
    • Hosokawa, K.1    Fujimura, R.K.2    Nomura, M.3
  • 61
    • 0038152834 scopus 로고    scopus 로고
    • Affinity purification of ribosomes with a lethal G2655C mutation in 23S rRNA that affects the translocation
    • Leonov,A.A., Sergiev,P.V., Bogdanov,A.A., Brimacombe,R. and Dontsova,O.A. (2003) Affinity purification of ribosomes with a lethal G2655C mutation in 23S rRNA that affects the translocation. J. Biol. Chem., 278, 25664-25670.
    • (2003) J. Biol. Chem , vol.278 , pp. 25664-25670
    • Leonov, A.A.1    Sergiev, P.V.2    Bogdanov, A.A.3    Brimacombe, R.4    Dontsova, O.A.5
  • 62
    • 33646495214 scopus 로고    scopus 로고
    • Ribosome dynamics: Insights from atomic structure modeling into cryo-electron microscopy maps
    • Mitra,K. and Frank,J. (2006) Ribosome dynamics: Insights from atomic structure modeling into cryo-electron microscopy maps. Annu. Rev. Biophys. Biomol. Struct., 35, 299-317.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 299-317
    • Mitra, K.1    Frank, J.2
  • 63
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • Moore,P.B. and Steitz,T.A. (2003) The structural basis of large ribosomal subunit function. Annu. Rev., Biochem., 72, 813-850.
    • (2003) Annu. Rev., Biochem , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 64
    • 14544268235 scopus 로고    scopus 로고
    • On the structural basis of peptide-bond formation and antibiotic resistance front atomic structures of the large ribosomal subunit
    • Steitz,T.A. (2005) On the structural basis of peptide-bond formation and antibiotic resistance front atomic structures of the large ribosomal subunit. FEBS Lett., 579, 955-958.
    • (2005) FEBS Lett , vol.579 , pp. 955-958
    • Steitz, T.A.1
  • 65
    • 0016838255 scopus 로고
    • A link between streptomycin and rifampicin mutation
    • Chakrabarti,S.L. and Gorini,L. (1975), A link between streptomycin and rifampicin mutation. Proc. Natl Acad Sci. USA, 72, 2084-2087.
    • (1975) Proc. Natl Acad Sci. USA , vol.72 , pp. 2084-2087
    • Chakrabarti, S.L.1    Gorini, L.2
  • 67
    • 33947240700 scopus 로고    scopus 로고
    • Ribosomal protein L3: Gatekeeper to the A-site
    • Moskauskas,A. and Dinman,J.D. (2007) Ribosomal protein L3: Gatekeeper to the A-site. Mol. Cell, 25, 877-888.
    • (2007) Mol. Cell , vol.25 , pp. 877-888
    • Moskauskas, A.1    Dinman, J.D.2
  • 69
    • 41149171234 scopus 로고    scopus 로고
    • Involvement of the N-terminal extension of ribosomal protein L3 in coordination of large subunit-associated functions
    • Submitted for publication
    • Meskauskas,A. and Dinman,J.D. (2007) Involvement of the N-terminal extension of ribosomal protein L3 in coordination of large subunit-associated functions. Submitted for publication.
    • (2007)
    • Meskauskas, A.1    Dinman, J.D.2


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