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Volumn 80, Issue , 2011, Pages 527-555

The mechanism of peptidyl transfer catalysis by the ribosome

Author keywords

entropy trap; induced fit; peptide bond formation; peptidyl transferase center; translation

Indexed keywords

AMIDE; AMINOACYL TRANSFER RNA; HYDROGEN; NITROGEN; NUCLEOPHILE; PEPTIDYLTRANSFERASE; RNA 23S; TRANSFER RNA; WATER;

EID: 79959411466     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-082108-165150     Document Type: Article
Times cited : (46)

References (124)
  • 1
    • 70349295276 scopus 로고    scopus 로고
    • Changes in transcript abundance relating to colony collapse disorder in honey bees (Apis mellifera)
    • Johnson RM, Evans JD, Robinson GE, Berenbaum MR. 2009. Changes in transcript abundance relating to colony collapse disorder in honey bees (Apis mellifera). Proc. Natl. Acad. Sci. USA 106:14790-795.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14790-14795
    • Johnson, R.M.1    Evans, J.D.2    Robinson, G.E.3    Berenbaum, M.R.4
  • 2
    • 0035451794 scopus 로고    scopus 로고
    • The once and future nanomachine
    • Whitesides GM. 2001. The once and future nanomachine. Sci. Am. 285:78-83.
    • (2001) Sci. Am. , vol.285 , pp. 78-83
    • Whitesides, G.M.1
  • 3
    • 0033966203 scopus 로고    scopus 로고
    • Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12
    • DOI 10.1074/jbc.275.2.890
    • Savelsbergh A, Mohr D, Wilden B, Wintermeyer W, Rodnina MV. 2000. Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12. J. Biol. Chem. 275:890-894. (Pubitemid 30051131)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 890-894
    • Savelsbergh, A.1    Mohr, D.2    Wilden, B.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 4
    • 0024841098 scopus 로고
    • Binding of the 3' terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation
    • Lill R, Robertson JM, WintermeyerW. 1989. Binding of the 3′ terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation. EMBO J. 8:3933-938. (Pubitemid 20016078)
    • (1989) EMBO Journal , vol.8 , Issue.12 , pp. 3933-3938
    • Lill, R.1    Robertson, J.M.2    Wintermeyer, W.3
  • 6
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • DOI 10.1038/385037a0
    • Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W. 1997. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385:37-41. (Pubitemid 27024544)
    • (1997) Nature , vol.385 , Issue.6611 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 7
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically competent intermediates in the translocation step of protein synthesis
    • DOI 10.1016/j.molcel.2007.01.014, PII S1097276507000366
    • Pan D, Kirillov SV, Cooperman BS. 2007. Kinetically competent intermediates in the translocation step of protein synthesis. Mol. Cell 25:519-529. (Pubitemid 46274443)
    • (2007) Molecular Cell , vol.25 , Issue.4 , pp. 519-529
    • Pan, D.1    Kirillov, S.V.2    Cooperman, B.S.3
  • 8
    • 0038433302 scopus 로고    scopus 로고
    • An Elongation Factor G-Induced Ribosome Rearrangement Precedes tRNA-mRNA Translocation
    • DOI 10.1016/S1097-2765(03)00230-2
    • Savelsbergh A, Katunin VI, Mohr D, Peske F, Rodnina MV, Wintermeyer W. 2003. An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation. Mol. Cell 11:1517-523. (Pubitemid 36776538)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 9
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis: The circe effect
    • Jencks WP. 1975. Binding energy, specificity, and enzymic catalysis: the circe effect. Adv. Enzymol. Relat. Areas Mol. Biol. 43:219-410.
    • (1975) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 13
    • 0032535207 scopus 로고    scopus 로고
    • Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E.coli ribosome
    • DOI 10.1093/emboj/17.24.7490
    • Pape T, Wintermeyer W, Rodnina MV. 1998. Complete kinetic mechanism of elongation factor Tudependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J. 17:7490-497. (Pubitemid 29002715)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 14
    • 33745071762 scopus 로고    scopus 로고
    • Peptide bond formation does not involve acid-base catalysis by ribosomal residues
    • DOI 10.1038/nsmb1091, PII N1091
    • Bieling P, Beringer M, Adio S, Rodnina MV. 2006. Peptide bond formation does not involve acid-base catalysis by ribosomal residues. Nat. Struct. Mol. Biol. 13:423-428. (Pubitemid 43881582)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.5 , pp. 423-428
    • Bieling, P.1    Beringer, M.2    Adio, S.3    Rodnina, M.V.4
  • 15
    • 29844448116 scopus 로고    scopus 로고
    • The interaction between C75 of tRNA and the A loop of the ribosome stimulates peptidyl transferase activity
    • DOI 10.1261/rna.2256706
    • Brunelle JL, Youngman EM, Sharma D, Green R. 2006. The interaction between C75 of tRNA and the A loop of the ribosome stimulates peptidyl transferase activity. RNA 12:33-39. (Pubitemid 43037451)
    • (2006) RNA , vol.12 , Issue.1 , pp. 33-39
    • Brunelle, J.L.1    Youngman, E.M.2    Sharma, D.3    Green, R.4
  • 16
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • DOI 10.1016/S1097-2765(02)00566-X
    • Katunin VI, Muth GW, Strobel SA, Wintermeyer W, Rodnina MV. 2002. Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome. Mol. Cell 10:339-346. (Pubitemid 35007348)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 339-346
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 17
    • 0001361466 scopus 로고
    • The mechanism of the aminolysis of methyl formate
    • Blackburn G, Jencks W. 1968. The mechanism of the aminolysis of methyl formate. J. Am. Chem. Soc. 90:2638-645.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 2638-2645
    • Blackburn, G.1    Jencks, W.2
  • 18
    • 0016405364 scopus 로고
    • Mechanism of aminolysis of acetate esters
    • Satterthwait A, Jencks W. 1974. Mechanism of aminolysis of acetate esters. J. Am. Chem. Soc. 96:7018-031.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 7018-7031
    • Satterthwait, A.1    Jencks, W.2
  • 19
    • 0000021289 scopus 로고
    • Secondary alpha-deuterium kinetic isotope effects and transition-state structures for the hydrolysis and hydrazinolysis reactions of formate esters
    • Bilkadi Z, de Lorimier R, Kirsch JF. 1975. Secondary alpha-deuterium kinetic isotope effects and transition-state structures for the hydrolysis and hydrazinolysis reactions of formate esters. J. Am. Chem. Soc. 97:4317-322.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4317-4322
    • Bilkadi, Z.1    De Lorimier, R.2    Kirsch, J.F.3
  • 20
    • 0000495223 scopus 로고
    • Kinetic isotope effects for reactions of methyl formate-methoxyl-18O
    • Sawyer CB, Kirsch JF. 1973. Kinetic isotope effects for reactions of methyl formate-methoxyl-18O. J. Am. Chem. Soc. 95:7375-381.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 7375-7381
    • Sawyer, C.B.1    Kirsch, J.F.2
  • 22
    • 84961979209 scopus 로고    scopus 로고
    • DFT studies on the structure and stability of zwitterionic tetrahedral intermediate in the aminolysis of esters
    • DOI 10.1016/j.cplett.2006.06.015, PII S000926140600858X
    • Sung DD, Koo IS, Yang K, Lee I. 2006. DFT studies on the structure and stability of zwitterionic tetrahedral intermediate in the aminolysis of esters. Chem. Phys. Lett. 426:280-284. (Pubitemid 44080151)
    • (2006) Chemical Physics Letters , vol.426 , Issue.4-6 , pp. 280-284
    • Sung, D.D.1    Koo, I.S.2    Yang, K.3    Lee, I.4
  • 23
    • 0034623527 scopus 로고    scopus 로고
    • Resolution of conflictingmechanistic observations in ester aminolysis. A warning on the qualitative prediction of isotope effects for reactive intermediates
    • Singleton DA, Merrigan SR. 2000. Resolution of conflictingmechanistic observations in ester aminolysis. A warning on the qualitative prediction of isotope effects for reactive intermediates. J. Am. Chem. Soc. 122:11035-036.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11035-11036
    • Singleton, D.A.1    Merrigan, S.R.2
  • 24
    • 84962374950 scopus 로고    scopus 로고
    • Computational study of the aminolysis of esters. The reaction of methylformate with ammonia
    • DOI 10.1021/jo0263723
    • Ilieva S, Galabov B, Musaev DG, Morokuma K, Schaefer HF. 2003. Computational study of the aminolysis of esters. The reaction of methylformate with ammonia. J. Org. Chem. 68:1496-502. (Pubitemid 36232514)
    • (2003) Journal of Organic Chemistry , vol.68 , Issue.4 , pp. 1496-1502
    • Ilieva, S.1    Galabov, B.2    Musaev, D.G.3    Morokuma, K.4    Schaefer III, H.F.5
  • 25
    • 58149142931 scopus 로고    scopus 로고
    • DFTstudy andMonte Carlo simulation on the aminolysis of XC(O)OCH3 (X = NH2, H, and CF3) with monomeric and dimeric ammonias
    • XiaX, Zhang C, Xue Y, Kim CK, YanG. 2008.DFTstudy andMonte Carlo simulation on the aminolysis of XC(O)OCH3 (X = NH2, H, and CF3) with monomeric and dimeric ammonias. J. Chem. Theory Comput. 4:1643-653.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 1643-1653
    • Xia, X.1    Zhang, C.2    Xue, Y.3    Kim, C.K.4    Yan, G.5
  • 27
    • 0034860631 scopus 로고    scopus 로고
    • Multiple isotope effects on the acyl group transfer reactions of amides and esters
    • DOI 10.1021/ar000054d
    • Marlier JF. 2001. Multiple isotope effects on the acyl group transfer reactions of amides and esters. Acc. Chem. Res. 34:283-290. (Pubitemid 32816465)
    • (2001) Accounts of Chemical Research , vol.34 , Issue.4 , pp. 283-290
    • Marlier, J.F.1
  • 28
    • 77951932920 scopus 로고    scopus 로고
    • Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal P-site substrate determined by kinetic isotope effects
    • Hiller DA, ZhongM, Singh V, Strobel SA. 2010. Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal P-site substrate determined by kinetic isotope effects. Biochemistry 49:3868-78.
    • (2010) Biochemistry , vol.49 , pp. 3868-3878
    • Hiller, D.A.1    Zhong, M.2    Singh, V.3    Strobel, S.A.4
  • 29
    • 14844352639 scopus 로고    scopus 로고
    • Kinetic isotope effect analysis of the ribosomal peptidyl transferase reaction
    • DOI 10.1021/bi047742f
    • Seila AC, Okuda K, Nunez S, Seila AF, Strobel SA. 2005. Kinetic isotope effect analysis of the ribosomal peptidyl transferase reaction. Biochemistry 44:4018-027. (Pubitemid 40358054)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 4018-4027
    • Seila, A.C.1    Okuda, K.2    Nunez, S.3    Seila, A.F.4    Strobel, S.A.5
  • 31
    • 17844385296 scopus 로고    scopus 로고
    • a of the ribosomal peptidyl transferase reaction utilizing a fluorinated puromycin derivative
    • DOI 10.1021/bi047419c
    • Okuda K, Seila AC, Strobel SA. 2005. Uncovering the enzymatic pKa of the ribosomal peptidyl transferase reaction utilizing a fluorinated puromycin derivative. Biochemistry 44:6675-684. (Pubitemid 40593818)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6675-6684
    • Okuda, K.1    Seila, A.C.2    Strobel, S.A.3
  • 32
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • DOI 10.1126/science.289.5481.920
    • Nissen P, Hansen J, Ban N, Moore PB, Steitz TA. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930. (Pubitemid 30659940)
    • (2000) Science , vol.289 , Issue.5481 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 33
    • 0034637102 scopus 로고    scopus 로고
    • A single adenosine with a neutral pK(a) in the ribosomal peptidyl transferase center
    • DOI 10.1126/science.289.5481.947
    • Muth GW, Ortoleva-Donnelly L, Strobel SA. 2000. A single adenosine with a neutral pKa in the ribosomal peptidyl transferase center. Science 289:947-950. (Pubitemid 30659946)
    • (2000) Science , vol.289 , Issue.5481 , pp. 947-950
    • Muth, G.W.1    Ortoleva-Donnelly, L.2    Strobel, S.A.3
  • 34
    • 3142727548 scopus 로고    scopus 로고
    • Exploration of the conserved A+C wobble pair within the ribosomal peptidyl transferase center using affinity purified mutant ribosomes
    • DOI 10.1093/nar/gkh672
    • Hesslein AE, Katunin VI, Beringer M, Kosek AB, Rodnina MV, Strobel SA. 2004. Exploration of the conserved A+C wobble pair within the ribosomal peptidyl transferase center using affinity purified mutant ribosomes. Nucleic Acids Res. 32:3760-770. (Pubitemid 39157723)
    • (2004) Nucleic Acids Research , vol.32 , Issue.12 , pp. 3760-3770
    • Hesslein, A.E.1    Katunin, V.I.2    Beringer, M.3    Kosek, A.B.4    Rodnina, M.V.5    Strobel, S.A.6
  • 35
    • 6044222469 scopus 로고    scopus 로고
    • The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation
    • DOI 10.1093/nar/gkh888
    • Bayfield MA, Thompson J, Dahlberg AE. 2004. The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation. Nucleic Acids Res. 32:5512-518. (Pubitemid 39545668)
    • (2004) Nucleic Acids Research , vol.32 , Issue.18 , pp. 5512-5518
    • Bayfield, M.A.1    Thompson, J.2    Dahlberg, A.E.3
  • 36
    • 0034757629 scopus 로고    scopus 로고
    • PH-dependent conformational flexibility within the ribosomal peptidyl transferase center
    • Muth GW, Chen L, Kosek AB, Strobel SA. 2001. pH-dependent conformational flexibility within the ribosomal peptidyl transferase center. RNA 7:1403-415. (Pubitemid 32973226)
    • (2001) RNA , vol.7 , Issue.10 , pp. 1403-1415
    • Muth, G.W.1    Chen, L.2    Kosek, A.B.3    Strobel, S.A.4
  • 37
    • 0034768574 scopus 로고    scopus 로고
    • PKa of adenine 2451 in the ribosomal peptidyl transferase center remains elusive
    • Xiong L, Polacek N, Sander P, B̈ottger EC, Mankin A. 2001. pKa of adenine 2451 in the ribosomal peptidyl transferase center remains elusive. RNA 7:1365-369. (Pubitemid 32973221)
    • (2001) RNA , vol.7 , Issue.10 , pp. 1365-1369
    • Xiong, L.1    Polacek, N.2    Sander, P.3    Bottger, E.C.4    Mankin, A.5
  • 39
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
    • DOI 10.1038/35078113
    • Polacek N, Gaynor M, Yassin A, Mankin AS. 2001. Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide. Nature 411:498-501. (Pubitemid 32494398)
    • (2001) Nature , vol.411 , Issue.6836 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 40
    • 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
    • DOI 10.1016/S0092-8674(04)00411-8, PII S0092867404004118
    • Youngman EM, Brunelle JL, Kochaniak AB, 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. (Pubitemid 38692525)
    • (2004) Cell , vol.117 , Issue.5 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 42
    • 0038359320 scopus 로고    scopus 로고
    • The G2447A mutation does not affect ionization of a ribosomal group taking part in peptide bond formation
    • DOI 10.1261/rna.5600503
    • Beringer M, Adio S, WintermeyerW, RodninaM. 2003. TheG2447A mutation does not affect ionization of a ribosomal group taking part in peptide bond formation. RNA 9:919-922. (Pubitemid 36899234)
    • (2003) RNA , vol.9 , Issue.8 , pp. 919-922
    • Beringer, M.1    Adio, S.2    Wintermeyer, W.3    Rodnina, M.V.4
  • 43
    • 33748559498 scopus 로고    scopus 로고
    • Nucleobase catalysis in ribozyme mechanism
    • DOI 10.1016/j.cbpa.2006.08.014, PII S1367593106001219, Analytical Techniques/Mechanisms
    • Bevilacqua PC, Yajima R. 2006. Nucleobase catalysis in ribozyme mechanism. Curr. Opin. Chem. Biol. 10:455-464. (Pubitemid 44375067)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 455-464
    • Bevilacqua, P.C.1    Yajima, R.2
  • 44
    • 0017018406 scopus 로고
    • The intrinsic pKa-values of functional groups in enzymes: Improper deductions from the pH-dependence of steady-state parameters
    • Knowles JR. 1976. The intrinsic pKa-values of functional groups in enzymes: improper deductions from the pH-dependence of steady-state parameters. CRC Crit. Rev. Biochem. 4:165-173.
    • (1976) CRC Crit. Rev. Biochem. , vol.4 , pp. 165-173
    • Knowles, J.R.1
  • 45
    • 0037145032 scopus 로고    scopus 로고
    • The path to perdition is paved with protons
    • DOI 10.1016/S0092-8674(02)00965-0
    • Green R, Lorsch JR. 2002. The path to perdition is paved with protons. Cell 110:665-668. (Pubitemid 35283956)
    • (2002) Cell , vol.110 , Issue.6 , pp. 665-668
    • Green, R.1    Lorsch, J.R.2
  • 46
    • 42449134886 scopus 로고    scopus 로고
    • Role of ribosomal protein L27 in peptidyl transfer
    • DOI 10.1021/bi8001874
    • Trobro S, Äqvist J. 2008. Role of ribosomal protein L27 in peptidyl transfer. Biochemistry 47:4898-906. (Pubitemid 351574996)
    • (2008) Biochemistry , vol.47 , Issue.17 , pp. 4898-4906
    • Trobro, S.1    Aqvist, J.2
  • 47
    • 33745633573 scopus 로고    scopus 로고
    • Rapid peptide bond formation on isolated 50S ribosomal subunits
    • DOI 10.1038/sj.embor.7400732, PII 7400732
    • Wohlgemuth I, BeringerM, RodninaMV. 2006. Rapid peptide bond formation on isolated 50S ribosomal subunits. EMBO Rep. 7:699-703. (Pubitemid 43986266)
    • (2006) EMBO Reports , vol.7 , Issue.7 , pp. 699-703
    • Wohlgemuth, I.1    Beringer, M.2    Rodnina, M.V.3
  • 48
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • DOI 10.1126/science.289.5481.905
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289:905-920. (Pubitemid 30659939)
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 49
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • DOI 10.1038/nature04152, PII N04152
    • Schmeing TM, Huang KS, Strobel SA, Steitz TA. 2005. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438:520-524. (Pubitemid 41742026)
    • (2005) Nature , vol.438 , Issue.7067 , pp. 520-524
    • Martin Schmeing, T.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 53
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller HF, Hoffarth V, Zimniak L. 1992. Unusual resistance of peptidyl transferase to protein extraction procedures. Science 256:1416-419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 55
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction
    • DOI 10.1016/j.molcel.2005.09.006, PII S1097276505016060
    • Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA. 2005. Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol. Cell 20:437-448. (Pubitemid 41572300)
    • (2005) Molecular Cell , vol.20 , Issue.3 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 58
    • 33748582906 scopus 로고    scopus 로고
    • Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements
    • DOI 10.1016/j.cell.2006.08.032, PII S0092867406011469
    • Korostelev A, Trakhanov S, Laurberg M, Noller HF. 2006. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126:1065-077. (Pubitemid 44380300)
    • (2006) Cell , vol.126 , Issue.6 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 59
    • 66149157000 scopus 로고    scopus 로고
    • Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
    • Voorhees RM, Weixlbaumer A, Loakes D, Kelley AC, Ramakrishnan V. 2009. Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nat. Struct. Mol. Biol. 16:528-533.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 528-533
    • Voorhees, R.M.1    Weixlbaumer, A.2    Loakes, D.3    Kelley, A.C.4    Ramakrishnan, V.5
  • 63
    • 77955786910 scopus 로고    scopus 로고
    • The role of the universally conserved A2450-C2063 base pair in the ribosomal peptidyl transferase center
    • Chirkova A, Erlacher MD, Clementi N, Zywicki M, Aigner M, Polacek N. 2010. The role of the universally conserved A2450-C2063 base pair in the ribosomal peptidyl transferase center. Nucleic Acids Res. 38:4844-855.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 4844-4855
    • Chirkova, A.1    Erlacher, M.D.2    Clementi, N.3    Zywicki, M.4    Aigner, M.5    Polacek, N.6
  • 65
    • 33745048734 scopus 로고    scopus 로고
    • Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer
    • DOI 10.1021/bi0605383
    • Trobro S, Äqvist J. 2006. Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer. Biochemistry 45:7049-056. (Pubitemid 43877393)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7049-7056
    • Trobro, S.1    Aqvist, J.2
  • 67
    • 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 MD, Lang K, Wotzel B, Rieder R, Micura R, 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. 128:4453-459.
    • (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
  • 69
    • 53249123416 scopus 로고    scopus 로고
    • Peptide-bond synthesis on the ribosome: No free vicinal hydroxy group required on the terminal ribose residue of peptidyl-tRNA
    • Koch M, Huang Y, Sprinzl M. 2008. Peptide-bond synthesis on the ribosome: no free vicinal hydroxy group required on the terminal ribose residue of peptidyl-tRNA. Angew. Chem. Int. Ed. Engl. 47:7242-245.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 7242-7245
    • Koch, M.1    Huang, Y.2    Sprinzl, M.3
  • 70
    • 0033957143 scopus 로고    scopus 로고
    • Substrate-assisted catalysis: Molecular basis and biological significance
    • Dall'Acqua W, Carter P. 2000. Substrate-assisted catalysis: molecular basis and biological significance. Protein Sci. 9:1-9. (Pubitemid 30070933)
    • (2000) Protein Science , vol.9 , Issue.1 , pp. 1-9
    • Dall'Acqua, W.1    Carter, P.2
  • 71
    • 33646568156 scopus 로고    scopus 로고
    • Participation of the tRNA A76 hydroxyl groups throughout translation
    • DOI 10.1021/bi060183n
    • Weinger JS, Strobel SA. 2006. Participation of the tRNA A76 hydroxyl groups throughout translation. Biochemistry 45:5939-948. (Pubitemid 43727085)
    • (2006) Biochemistry , vol.45 , Issue.19 , pp. 5939-5948
    • Weinger, J.S.1    Strobel, S.A.2
  • 72
    • 33646141185 scopus 로고    scopus 로고
    • The syn-oriented 2-OH provides a favorable proton transfer geometry in 1, 2-diol monoester aminolysis: Implications for the ribosome mechanism
    • Rangelov MA, Vayssilov GN, Yomtova VM, Petkov DD. 2006. The syn-oriented 2-OH provides a favorable proton transfer geometry in 1, 2-diol monoester aminolysis: implications for the ribosome mechanism. J. Am. Chem. Soc. 128:4964-965.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4964-4965
    • Rangelov, M.A.1    Vayssilov, G.N.2    Yomtova, V.M.3    Petkov, D.D.4
  • 73
    • 23944472625 scopus 로고    scopus 로고
    • What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome?
    • DOI 10.1021/bi0509806
    • Sharma PK, Xiang Y, Kato M, Warshel A. 2005. What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome? Biochemistry 44:11307-314. (Pubitemid 41209066)
    • (2005) Biochemistry , vol.44 , Issue.34 , pp. 11307-11314
    • Sharma, P.K.1    Xiang, Y.2    Kato, M.3    Warshel, A.4
  • 74
    • 34047227549 scopus 로고    scopus 로고
    • The rate enhancement produced by the ribosome: An improved model
    • DOI 10.1021/bi602600p
    • Schroeder GK, Wolfenden R. 2007. The rate enhancement produced by the ribosome: an improved model. Biochemistry 46:4037-044. (Pubitemid 46536067)
    • (2007) Biochemistry , vol.46 , Issue.13 , pp. 4037-4044
    • Schroeder, G.K.1    Wolfenden, R.2
  • 75
    • 50149106750 scopus 로고    scopus 로고
    • Transition state chirality and role of the vicinal hydroxyl in the ribosomal peptidyl transferase reaction
    • Huang KS, Carrasco N, Pfund E, Strobel SA. 2008. Transition state chirality and role of the vicinal hydroxyl in the ribosomal peptidyl transferase reaction. Biochemistry 47:8822-827.
    • (2008) Biochemistry , vol.47 , pp. 8822-8827
    • Huang, K.S.1    Carrasco, N.2    Pfund, E.3    Strobel, S.A.4
  • 76
    • 59649095963 scopus 로고    scopus 로고
    • A short guide formolecular dynamics simulations ofRNAsystems
    • Hashem Y, Auffinger P. 2009. A short guide formolecular dynamics simulations ofRNAsystems. Methods 47:187-197.
    • (2009) Methods , vol.47 , pp. 187-197
    • Hashem, Y.1    Auffinger, P.2
  • 77
    • 76649094618 scopus 로고    scopus 로고
    • The transition state for peptide bond formation reveals the ribosome as a water trap
    • WallinG, Äqvist J. 2010. The transition state for peptide bond formation reveals the ribosome as a water trap. Proc. Natl. Acad. Sci. USA 107:1888-893.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1888-1893
    • Wallin, G.1    Äqvist, J.2
  • 78
    • 43149098292 scopus 로고    scopus 로고
    • The role of 23s ribosomal RNA residue A2451 in peptide bond synthesis revealed by atomic mutagenesis
    • DOI 10.1016/j.chembiol.2008.03.014, PII S1074552108001257
    • Lang K, Erlacher M, Wilson DN, Micura R, Polacek N. 2008. The role of 23S ribosomal RNA residue A2451 in peptide bond synthesis revealed by atomic mutagenesis. Chem. Biol. 15:485-492. (Pubitemid 351645110)
    • (2008) Chemistry and Biology , vol.15 , Issue.5 , pp. 485-492
    • Lang, K.1    Erlacher, M.2    Wilson, D.N.3    Micura, R.4    Polacek, N.5
  • 79
    • 34548587149 scopus 로고    scopus 로고
    • An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination
    • DOI 10.1093/nar/gkm539
    • Amort M, Wotzel B, Bakowska-Zywicka K, Erlacher MD, Micura R, Polacek N. 2007. An intact ribose moiety at A2602 of 23S rRNA is key to trigger peptidyl-tRNA hydrolysis during translation termination. Nucleic Acids Res. 35:5130-140. (Pubitemid 47394197)
    • (2007) Nucleic Acids Research , vol.35 , Issue.15 , pp. 5130-5140
    • Amort, M.1    Wotzel, B.2    Bakowska-Zywicka, K.3    Erlacher, M.D.4    Micura, R.5    Polacek, N.6
  • 80
    • 37349113090 scopus 로고    scopus 로고
    • Ribozyme catalysis revisited: Is water involved?
    • DOI 10.1016/j.molcel.2007.12.001, PII S1097276507008234
    • Walter NG. 2007. Ribozyme catalysis revisited: Is water involved? Mol. Cell 28:923-929. (Pubitemid 350297026)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 923-929
    • Walter, N.G.1
  • 81
    • 0345099498 scopus 로고    scopus 로고
    • Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity
    • DOI 10.1093/nar/gkg842
    • Dorner S, Panuschka C, Schmid W, Barta A. 2003. Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity. Nucleic Acids Res. 31:6536-542. (Pubitemid 37508758)
    • (2003) Nucleic Acids Research , vol.31 , Issue.22 , pp. 6536-6542
    • Dorner, S.1    Panuschka, C.2    Schmid, W.3    Barta, A.4
  • 82
    • 0033592361 scopus 로고    scopus 로고
    • A possible mechanism of peptide bond formation on ribosome without mediation of peptidyl transferase
    • DOI 10.1006/jtbi.1999.0987
    • Das GK, Bhattacharyya D, Burma DP. 1999. A possible mechanism of peptide bond formation on ribosome without mediation of peptidyl transferase. J. Theor. Biol. 200:193-205. (Pubitemid 29481601)
    • (1999) Journal of Theoretical Biology , vol.200 , Issue.2 , pp. 193-205
    • Das, G.K.1    Bhattacharyya, D.2    Burma, D.P.3
  • 83
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • DOI 10.1038/342142a0
    • Moazed D, Noller HF. 1989. Intermediate states in the movement of transfer RNA in the ribosome. Nature 342:142-148. (Pubitemid 19277015)
    • (1989) Nature , vol.342 , Issue.6246 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 84
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome
    • Samaha RR, Green R, Noller HF. 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
  • 85
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A site
    • Kim DF, Green R. 1999. Base-pairing between 23S rRNA and tRNA in the ribosomal A site. Mol. Cell 4:859-864.
    • (1999) Mol. Cell , vol.4 , pp. 859-864
    • Kim, D.F.1    Green, R.2
  • 87
    • 36849129335 scopus 로고
    • The absolute rate of reactions in condensed phases
    • Wynne-Jones WFK, Eyring H. 1935. The absolute rate of reactions in condensed phases. J. Chem. Phys. 3:492-502.
    • (1935) J. Chem. Phys. , vol.3 , pp. 492-502
    • Wfk, W.1    Eyring, H.2
  • 88
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page MI, Jencks WP. 1971. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc. Natl. Acad. Sci. USA 68:1678-683.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 92
    • 44449089912 scopus 로고    scopus 로고
    • The kinetics of ribosomal peptidyl transfer revisited
    • DOI 10.1016/j.molcel.2008.04.010, PII S1097276508002931
    • Johansson M, Bouakaz E, Lovmar M, Ehrenberg M. 2008. The kinetics of ribosomal peptidyl transfer revisited. Mol. Cell 30:589-598. (Pubitemid 351755061)
    • (2008) Molecular Cell , vol.30 , Issue.5 , pp. 589-598
    • Johansson, M.1    Bouakaz, E.2    Lovmar, M.3    Ehrenberg, M.4
  • 93
    • 55549118938 scopus 로고    scopus 로고
    • Kinetic and thermodynamic studies of peptidyltransferase in ribosomes from the extreme thermophile Thermus thermophilus
    • Rodriguez-Correa D, Dahlberg AE. 2008. Kinetic and thermodynamic studies of peptidyltransferase in ribosomes from the extreme thermophile Thermus thermophilus. RNA 14:2314-318.
    • (2008) RNA , vol.14 , pp. 2314-2318
    • Rodriguez-Correa, D.1    Dahlberg, A.E.2
  • 94
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz JD. 1995. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 95
    • 0014126461 scopus 로고
    • Polypeptide chain termination in vitro: Isolation of a release factor
    • CapecchiMR. 1967. Polypeptide chain termination in vitro: isolation of a release factor. Proc. Natl. Acad. Sci. USA 58:1144-151.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.58 , pp. 1144-1151
    • Capecchi, M.R.1
  • 98
    • 0028305727 scopus 로고
    • A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity
    • Moffat JG, Tate WP. 1994. A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity. J. Biol. Chem. 269:18899-903. (Pubitemid 24226204)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.29 , pp. 18899-18903
    • Moffat, J.G.1    Tate, W.P.2
  • 99
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • DOI 10.1016/S0092-8674(01)00508-6
    • Zavialov AV, Buckingham RH, EhrenbergM. 2001. A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107:115-124. (Pubitemid 32972042)
    • (2001) Cell , vol.107 , Issue.1 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 100
    • 33744993160 scopus 로고    scopus 로고
    • In Vitro Reconstitution of Eukaryotic Translation Reveals Cooperativity between Release Factors eRF1 and eRF3
    • DOI 10.1016/j.cell.2006.04.035, PII S009286740600585X
    • Alkalaeva EZ, Pisarev AV, Frolova LY, Kisselev LL, Pestova TV. 2006. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125:1125-136. (Pubitemid 43866201)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 101
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song H, Mugnier P, Das AK, Webb HM, Evans DR, et al. 2000. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100:311-321. (Pubitemid 30353087)
    • (2000) Cell , vol.100 , Issue.3 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8
  • 102
    • 0035697089 scopus 로고    scopus 로고
    • Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1
    • DOI 10.1016/S1097-2765(01)00415-4
    • Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M. 2001. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol. Cell 8:1375-382. (Pubitemid 34085006)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1375-1382
    • Vestergaard, B.1    Van, L.B.2    Andersen, G.R.3    Nyborg, J.4    Buckingham, R.H.5    Kjeldgaard, M.6
  • 104
    • 29244487090 scopus 로고    scopus 로고
    • Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon
    • DOI 10.1016/j.cell.2005.09.039, PII S0092867405011682
    • Petry S, Brodersen DE, Murphy FV 4th, Dunham CM, Selmer M, et al. 2005. Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon. Cell 123:1255-266. (Pubitemid 41821783)
    • (2005) Cell , vol.123 , Issue.7 , pp. 1255-1266
    • Petry, S.1    Brodersen, D.E.2    Murphy IV, F.V.3    Dunham, C.M.4    Selmer, M.5    Tarry, M.J.6    Kelley, A.C.7    Ramakrishnan, V.8
  • 105
    • 70849098012 scopus 로고    scopus 로고
    • Multistart simulated annealing refinement of the crystal structure of the 70S ribosome
    • Korostelev A, Laurberg M, Noller HF. 2009. Multistart simulated annealing refinement of the crystal structure of the 70S ribosome. Proc. Natl. Acad. Sci. USA 106:18195-200.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18195-18200
    • Korostelev, A.1    Laurberg, M.2    Noller, H.F.3
  • 106
    • 55849143658 scopus 로고    scopus 로고
    • Insights into translational termination from the structure of RF2 bound to the ribosome
    • Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, et al. 2008. Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322:953-956.
    • (2008) Science , vol.322 , pp. 953-956
    • Weixlbaumer, A.1    Jin, H.2    Neubauer, C.3    Voorhees, R.M.4    Petry, S.5
  • 107
    • 55549147922 scopus 로고    scopus 로고
    • Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3′-hydroxyl group of A76 of the unacylated A-site tRNA
    • SimonovicM, Steitz TA. 2008. Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3′-hydroxyl group of A76 of the unacylated A-site tRNA. RNA 14:2372-378.
    • (2008) RNA , vol.14 , pp. 2372-2378
    • Simonovic, M.1    Steitz, T.A.2
  • 108
    • 65349134642 scopus 로고    scopus 로고
    • Does glutaminemethylation affect the intrinsic conformation of the universally conserved GGQ motif in ribosomal release factors?
    • AnderM, Äqvist J. 2009.Does glutaminemethylation affect the intrinsic conformation of the universally conserved GGQ motif in ribosomal release factors? Biochemistry 48:3483-489.
    • (2009) Biochemistry , vol.48 , pp. 3483-3489
    • Ander, M.1    Äqvist, J.2
  • 109
    • 34548227759 scopus 로고    scopus 로고
    • A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis
    • DOI 10.1016/j.molcel.2007.06.032, PII S1097276507004443
    • Trobro S, Äqvist J. 2007. A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis. Mol. Cell 27:758-766. (Pubitemid 47333221)
    • (2007) Molecular Cell , vol.27 , Issue.5 , pp. 758-766
    • Trobro, S.1    Aqvist, J.2
  • 110
    • 72749108166 scopus 로고    scopus 로고
    • Mechanismof the translation termination reaction on the ribosome
    • Trobro S, Äqvist J. 2009.Mechanismof the translation termination reaction on the ribosome. Biochemistry 48:11296-303.
    • (2009) Biochemistry , vol.48 , pp. 11296-11303
    • Trobro, S.1    Äqvist, J.2
  • 112
    • 35648950403 scopus 로고    scopus 로고
    • Two distinct components of release factor function uncovered by nucleophile partitioning analysis
    • DOI 10.1016/j.molcel.2007.09.007, PII S109727650700617X
    • Shaw JJ, Green R. 2007. Two distinct components of release factor function uncovered by nucleophile partitioning analysis. Mol. Cell 28:458-467. (Pubitemid 350030565)
    • (2007) Molecular Cell , vol.28 , Issue.3 , pp. 458-467
    • Shaw, J.J.1    Green, R.2
  • 113
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • DOI 10.1016/S1097-2765(02)00691-3
    • Zavialov AV, Mora L, Buckingham RH, EhrenbergM. 2002. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell 10:789-798. (Pubitemid 35335634)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 114
    • 33751083368 scopus 로고    scopus 로고
    • A conserved base-pair between tRNA and 23 S rRNA in the peptidyl transferase center is important for peptide release
    • DOI 10.1016/j.jmb.2006.09.040, PII S0022283606012460
    • Feinberg JS, Joseph S. 2006. A conserved base-pair between tRNA and 23 S rRNA in the peptidyl transferase center is important for peptide release. J. Mol. Biol. 364:1010-020. (Pubitemid 44765038)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.5 , pp. 1010-1020
    • Feinberg, J.S.1    Joseph, S.2
  • 115
    • 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
    • DOI 10.1016/S1097-2765(02)00825-0, PII S1097276502008250
    • Polacek N, Gomez MJ, Ito K, Xiong L, Nakamura Y, 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. (Pubitemid 36126594)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 103-112
    • Polacek, N.1    Gomez, M.J.2    Ito, K.3    Xiong, L.4    Nakamura, Y.5    Mankin, A.6
  • 116
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class I polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • DOI 10.1017/S135583829999043X
    • Frolova LY, Tsivkovskii RY, Sivolobova GF, Oparina NY, Serpinsky OI, et al. 1999. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5:1014-020. (Pubitemid 29365331)
    • (1999) RNA , vol.5 , Issue.8 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6    Tatkov, S.I.7    Kisselev, L.L.8
  • 117
    • 0347517767 scopus 로고    scopus 로고
    • Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03799.x
    • Mora L, Zavialov A, Ehrenberg M, Buckingham RH. 2003. Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli. Mol. Microbiol. 50:1467-476. (Pubitemid 38010445)
    • (2003) Molecular Microbiology , vol.50 , Issue.5 , pp. 1467-1476
    • Mora, L.1    Zavialov, A.2    Ehrenberg, M.3    Buckingham, R.H.4
  • 118
    • 0035476654 scopus 로고    scopus 로고
    • Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition
    • Seit-Nebi A, Frolova L, Justesen J, Kisselev L. 2001. Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition. Nucleic Acids Res. 29:3982-987. (Pubitemid 32962688)
    • (2001) Nucleic Acids Research , vol.29 , Issue.19 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 120
    • 47949094068 scopus 로고    scopus 로고
    • Peptide release on the ribosome depends critically on the 2′ OH of the peptidyl-tRNA substrate
    • Brunelle JL, Shaw JJ, Youngman EM, Green R. 2008. Peptide release on the ribosome depends critically on the 2′ OH of the peptidyl-tRNA substrate. RNA 14:1526-531.
    • (2008) RNA , vol.14 , pp. 1526-1531
    • Brunelle, J.L.1    Shaw, J.J.2    Youngman, E.M.3    Green, R.4
  • 121
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FV 4th, et al. 2009. The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326:688-694.
    • (2009) Science , vol.326 , pp. 688-694
    • Schmeing, T.M.1    Voorhees, R.M.2    Kelley, A.C.3    Gao, Y.G.4    Murphy IV, F.V.5
  • 122
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • DOI 10.1038/nrm2352, PII NRM2352
    • Steitz TA. 2008. A structural understanding of the dynamic ribosome machine. Nat. Rev. Mol. Cell Biol. 9:242-253. (Pubitemid 351301830)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 242-253
    • Steitz, T.A.1
  • 123
    • 0016405364 scopus 로고
    • Mechanism of aminolysis of acetate esters
    • Satterthwait AC, Jencks WP. 1974. Mechanism of aminolysis of acetate esters. J. Am. Chem. Soc. 96:7018-31.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 7018-7031
    • Satterthwait, A.C.1    Jencks, W.P.2
  • 124
    • 77952685666 scopus 로고    scopus 로고
    • Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release
    • Jin H, Kelley AC, Loakes D, Ramakrishnan V. 2010. Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release. Proc. Natl. Acad. Sci. USA 107:8593-98
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8593-8598
    • Jin, H.1    Kelley, A.C.2    Loakes, D.3    Ramakrishnan, V.4


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