메뉴 건너뛰기




Volumn 37, Issue 4, 2009, Pages 1202-1210

Specificity of the ribosomal A site for aminoacyl-tRNAs

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINOACYL TRANSFER RNA; ARGININE; BACTERIAL RNA; DEOXYRIBONUCLEOTIDE; GLUTAMIC ACID; GLYCINE; ISOLEUCINE; LYSINE; MESSENGER RNA; METHIONINE; PHENYLALANINE; THREONINE; TRYPTOPHAN; TYROSINE; VALINE;

EID: 62549083518     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn1040     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 9744230656 scopus 로고    scopus 로고
    • Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites
    • Fahlman,R.P., Dale,T. and Uhlenbeck,O.C. (2004) Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites. Mol. Cell, 16, 799-805.
    • (2004) Mol. Cell , vol.16 , pp. 799-805
    • Fahlman, R.P.1    Dale, T.2    Uhlenbeck, O.C.3
  • 2
    • 46149104347 scopus 로고    scopus 로고
    • Different aa-tRNAs are selected uniformly on the ribosome
    • Ledoux,S. and Uhlenbeck,O.C. (2008) Different aa-tRNAs are selected uniformly on the ribosome. Mol. Cell, 31, 114-123.
    • (2008) Mol. Cell , vol.31 , pp. 114-123
    • Ledoux, S.1    Uhlenbeck, O.C.2
  • 4
    • 0019873831 scopus 로고
    • Stereochemical control of ribosomal peptidyltransferase reaction. Role of amino acid side-chain orientation of acceptor substrate
    • Bhuta,A., Quiggle,K., Ott,T., Ringer,D. and Chladek,S. (1981) Stereochemical control of ribosomal peptidyltransferase reaction. Role of amino acid side-chain orientation of acceptor substrate. Biochemistry, 20, 8-15.
    • (1981) Biochemistry , vol.20 , pp. 8-15
    • Bhuta, A.1    Quiggle, K.2    Ott, T.3    Ringer, D.4    Chladek, S.5
  • 5
    • 0037668349 scopus 로고    scopus 로고
    • The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes
    • Starck,S.R., Qi,X., Olsen,B.N. and Roberts,R.W. (2003) The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes. J. Am. Chem. Soc., 125, 8090-8091.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8090-8091
    • Starck, S.R.1    Qi, X.2    Olsen, B.N.3    Roberts, R.W.4
  • 6
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen,P., Hansen,J., Ban,N., Moore,P.B. and Steitz,T.A. (2000) The structural basis of ribosome activity in peptide bond synthesis. Science, 289, 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 8
    • 27144554014 scopus 로고    scopus 로고
    • Binding of misacylated tRNAs to the ribosomal A site
    • Dale,T. and Uhlenbeck,O.C. (2005) Binding of misacylated tRNAs to the ribosomal A site. RNA, 11, 1610-1615.
    • (2005) RNA , vol.11 , pp. 1610-1615
    • Dale, T.1    Uhlenbeck, O.C.2
  • 10
    • 0037133662 scopus 로고    scopus 로고
    • The tRNA specificity of thermus thermophilus EF-Tu
    • Asahara,H. and Uhlenbeck,O.C. (2002) The tRNA specificity of thermus thermophilus EF-Tu. Proc. Natl Acad. Sci. USA, 99, 3499-3504.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3499-3504
    • Asahara, H.1    Uhlenbeck, O.C.2
  • 11
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson,J.R. and Uhlenbeck,O.C. (1988) Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl Acad. Sci. USA, 85, 1033-1037.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 12
    • 2442697841 scopus 로고    scopus 로고
    • The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid
    • Dale,T., Sanderson,L.E. and Uhlenbeck,O.C. (2004) The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid. Biochemistry, 43, 6159-6166.
    • (2004) Biochemistry , vol.43 , pp. 6159-6166
    • Dale, T.1    Sanderson, L.E.2    Uhlenbeck, O.C.3
  • 14
    • 0035958587 scopus 로고    scopus 로고
    • The path of messenger RNA through the ribosome
    • Yusupova,G.Z., Yusupov,M.M., Cate,J.H. and Noller,H.F. (2001) The path of messenger RNA through the ribosome. Cell, 106, 233-241.
    • (2001) Cell , vol.106 , pp. 233-241
    • Yusupova, G.Z.1    Yusupov, M.M.2    Cate, J.H.3    Noller, H.F.4
  • 15
    • 0031823330 scopus 로고    scopus 로고
    • A new assay for tRNA aminoacylation kinetics
    • Wolfson,A.D., Pleiss,J.A. and Uhlenbeck,O.C. (1998) A new assay for tRNA aminoacylation kinetics. RNA, 4, 1019-1023.
    • (1998) RNA , vol.4 , pp. 1019-1023
    • Wolfson, A.D.1    Pleiss, J.A.2    Uhlenbeck, O.C.3
  • 16
    • 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
  • 17
    • 2942592157 scopus 로고    scopus 로고
    • Contribution of the esterified amino acid to the binding of aminoacylated tRNAs to the ribosomal P- and A-sites
    • Fahlman,R.P. and Uhlenbeck,O.C. (2004) Contribution of the esterified amino acid to the binding of aminoacylated tRNAs to the ribosomal P- and A-sites. Biochemistry, 43, 7575-7583.
    • (2004) Biochemistry , vol.43 , pp. 7575-7583
    • Fahlman, R.P.1    Uhlenbeck, O.C.2
  • 18
    • 0033762347 scopus 로고    scopus 로고
    • Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome
    • Semenkov,Y.P., Rodnina,M.V. and Wintermeyer,W. (2000) Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome. Nat. Struct. Biol., 7, 1027-1031.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1027-1031
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 19
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites
    • Moazed,D. and Noller,H.F. (1989) Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites. Cell, 57, 585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 20
    • 0001358802 scopus 로고
    • RNA codewords and protein synthesis. The effect of trinucleotides upon the binding of sRNA to ribosomes
    • Nirenberg,M. and Leder,P. (1964) RNA codewords and protein synthesis. The effect of trinucleotides upon the binding of sRNA to ribosomes. Science, 145, 1399-1407.
    • (1964) Science , vol.145 , pp. 1399-1407
    • Nirenberg, M.1    Leder, P.2
  • 21
    • 0347623198 scopus 로고    scopus 로고
    • Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions
    • Konevega,A.L., Soboleva,N.G., Makhno,V.I., Semenkov,Y.P., Wintermeyer,W., Rodnina,M.V. and Katunin,V.I. (2004) Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactions. RNA, 10, 90-101.
    • (2004) RNA , vol.10 , pp. 90-101
    • Konevega, A.L.1    Soboleva, N.G.2    Makhno, V.I.3    Semenkov, Y.P.4    Wintermeyer, W.5    Rodnina, M.V.6    Katunin, V.I.7
  • 22
    • 33845995459 scopus 로고    scopus 로고
    • Ala with modified uridine in the wobble position
    • Ala with modified uridine in the wobble position. Mol. Cell, 25, 167-174.
    • (2007) Mol. Cell , vol.25 , pp. 167-174
    • Kothe, U.1    Rodnina, M.V.2
  • 23
    • 0036809730 scopus 로고    scopus 로고
    • Universally conserved interactions between the ribosome and the anticodon stem-loop of A site tRNA important for translocation
    • Phelps,S.S., Jerinic,O. and Joseph,S. (2002) Universally conserved interactions between the ribosome and the anticodon stem-loop of A site tRNA important for translocation. Mol. Cell, 10, 799-807.
    • (2002) Mol. Cell , vol.10 , pp. 799-807
    • Phelps, S.S.1    Jerinic, O.2    Joseph, S.3
  • 24
    • 29444458984 scopus 로고    scopus 로고
    • Quantitative analysis of deoxynucleotide substitutions in the codonanticodon helix
    • Fahlman,R.P., Olejniczak,M. and Uhlenbeck,O.C. (2006) Quantitative analysis of deoxynucleotide substitutions in the codonanticodon helix. J. Mol. Biol., 355, 887-892.
    • (2006) J. Mol. Biol , vol.355 , pp. 887-892
    • Fahlman, R.P.1    Olejniczak, M.2    Uhlenbeck, O.C.3
  • 25
    • 0034083601 scopus 로고    scopus 로고
    • E.ects of anticodon 2'-O-methylations on tRNA codon recognition in an Escherichia coli cell-free translation
    • Satoh,A., Takai,K., Ouchi,R., Yokoyama,S. and Takaku,H. (2000) E.ects of anticodon 2'-O-methylations on tRNA codon recognition in an Escherichia coli cell-free translation. RNA, 6, 680-686.
    • (2000) RNA , vol.6 , pp. 680-686
    • Satoh, A.1    Takai, K.2    Ouchi, R.3    Yokoyama, S.4    Takaku, H.5
  • 26
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle,J.M., Murphy,F.V., Tarry,M.J. and Ramakrishnan,V. (2002) Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell, 111, 721-732.
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 27
    • 0015505549 scopus 로고
    • Factor-dependent release of ribosomes from messenger RNA. Requirement for two heat-stable factors
    • Hirashima,A. and Kaji,A. (1972) Factor-dependent release of ribosomes from messenger RNA. Requirement for two heat-stable factors. J. Mol. Biol., 65, 43-58.
    • (1972) J. Mol. Biol , vol.65 , pp. 43-58
    • Hirashima, A.1    Kaji, A.2
  • 28
    • 0023028723 scopus 로고
    • Pressure dependence of equilibria and kinetics of Escherichia coli ribosomal subunit association
    • Pande,C. and Wishnia,A. (1986) Pressure dependence of equilibria and kinetics of Escherichia coli ribosomal subunit association. J. Biol. Chem., 261, 6272-6278.
    • (1986) J. Biol. Chem , vol.261 , pp. 6272-6278
    • Pande, C.1    Wishnia, A.2
  • 29
    • 47049098691 scopus 로고    scopus 로고
    • Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting
    • Pavlov,M.Y., Antoun,A., Lovmar,M. and Ehrenberg,M. (2008) Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting. EMBO J., 27, 1706-1717.
    • (2008) EMBO J , vol.27 , pp. 1706-1717
    • Pavlov, M.Y.1    Antoun, A.2    Lovmar, M.3    Ehrenberg, M.4
  • 30
    • 28544452248 scopus 로고    scopus 로고
    • An induced fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing,T., Huang,K., Strobel,S. and Steitz,T. (2005) An induced fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature, 438, 520-524.
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.1    Huang, K.2    Strobel, S.3    Steitz, T.4
  • 31
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev,A., Trakhanov,S., Laurberg,M. and Noller,H.F. (2006) Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell, 126, 1065-1077.
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 32
    • 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
    • Pape,T., Wintermeyer,W. and Rodnina,M.V. (1998) Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J., 17, 7490-7497.
    • (1998) EMBO J , vol.17 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 35
    • 1842420639 scopus 로고    scopus 로고
    • Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome
    • Gromadski,K.B. and Rodnina,M.V. (2004) Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome. Nature Struct. Mol. Biol., 11, 316-322.
    • (2004) Nature Struct. Mol. Biol , vol.11 , pp. 316-322
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 36
    • 0842267211 scopus 로고    scopus 로고
    • Kinetic determinants of high-fidelity tRNA discrimination on the ribosome
    • Gromadski,K.B. and Rodnina,M.V. (2004) Kinetic determinants of high-fidelity tRNA discrimination on the ribosome. Mol. Cell, 13, 191-200.
    • (2004) Mol. Cell , vol.13 , pp. 191-200
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 37
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape,T., Wintermeyer,W. and Rodnina,M. (1999) Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18, 3800-3807.
    • (1999) EMBO J , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 38
    • 0033961143 scopus 로고    scopus 로고
    • Conformational switch in the decoding region of 16S rRNA during aminoacyl-tRNA selection on the ribosome
    • Pape,T., Wintermeyer,W. and Rodnina,M.V. (2000) Conformational switch in the decoding region of 16S rRNA during aminoacyl-tRNA selection on the ribosome. Nature Struct. Biol., 7, 104-107.
    • (2000) Nature Struct. Biol , vol.7 , pp. 104-107
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 39
    • 33747881692 scopus 로고    scopus 로고
    • Alignment/misalignment hypothesis for tRNA selection by the ribosome
    • Sanbonmatsu,K.Y. (2006) Alignment/misalignment hypothesis for tRNA selection by the ribosome. Biochimie, 88, 1075-1089.
    • (2006) Biochimie , vol.88 , pp. 1075-1089
    • Sanbonmatsu, K.Y.1
  • 40
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle,J.M. and Ramakrishnan,V. (2005) Structural insights into translational fidelity. Annu. Rev. Biochem., 74, 129-177.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 41
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland,D.E. (1958) Application of a theory of enzyme specificity to protein synthesis. Proc. Natl Acad. Sci. USA, 44, 98-104.
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 42
    • 31544454704 scopus 로고    scopus 로고
    • A uniform response to mismatches in codon-anticodon complexes ensures ribosomal fidelity
    • Gromadski,K.B., Daviter,T. and Rodnina,M.V. (2006) A uniform response to mismatches in codon-anticodon complexes ensures ribosomal fidelity. Mol. Cell, 21, 369-377.
    • (2006) Mol. Cell , vol.21 , pp. 369-377
    • Gromadski, K.B.1    Daviter, T.2    Rodnina, M.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.