메뉴 건너뛰기




Volumn 108, Issue 13, 2011, Pages 5215-5220

Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINOACYL TRANSFER RNA; ELONGATION FACTOR TU;

EID: 79955113244     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1102128108     Document Type: Article
Times cited : (84)

References (47)
  • 1
    • 77449133028 scopus 로고    scopus 로고
    • Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu
    • Agirrezabala X, Frank J (2009) Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu. Q Rev Biophys 42:159-200.
    • (2009) Q Rev Biophys , vol.42 , pp. 159-200
    • Agirrezabala, X.1    Frank, J.2
  • 3
    • 0034923932 scopus 로고    scopus 로고
    • Fidelity of aminoacyl-tRNA selection on the ribosome: Kinetic and structural mechanisms
    • DOI 10.1146/annurev.biochem.70.1.415
    • Rodnina MV, Wintermeyer W (2001) Fidelity of aminoacyl-tRNA selection on the ribosome: Kinetic and structural mechanisms. Annu Rev Biochem 70:415-435. (Pubitemid 32662216)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 415-435
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 5
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: Lessons from protein synthesis
    • Zaher HS, Green R (2009) Fidelity at the molecular level: Lessons from protein synthesis. Cell 136:746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 6
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing TM, Ramakrishnan V (2009) What recent ribosome structures have revealed about the mechanism of translation. Nature 461:1234-1242.
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 7
    • 0021344828 scopus 로고
    • Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP
    • Louie A, Ribeiro NS, Reid BR, Jurnak F (1984) Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP. J Biol Chem 259:5010-5016. (Pubitemid 14140600)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.8 , pp. 5010-5016
    • Louie, A.1    Ribeiro, N.S.2    Reid, B.R.3    Jurnak, F.4
  • 8
    • 23944520820 scopus 로고    scopus 로고
    • Predicting the binding affinities of misacylated tRNAs for Thermus thermophilus EF-Tu·GTP
    • DOI 10.1021/bi050204y
    • Asahara H, Uhlenbeck OC (2005) Predicting the binding affinities ofmisacylated tRNAs for Thermus thermophilus EF-Tu.GTP. Biochemistry 44:11254-11261. (Pubitemid 41209060)
    • (2005) Biochemistry , vol.44 , Issue.33 , pp. 11254-11261
    • Asahara, H.1    Uhlenbeck, O.C.2
  • 11
    • 2442697841 scopus 로고    scopus 로고
    • The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid
    • DOI 10.1021/bi036290o
    • Dale T, Sanderson LE, Uhlenbeck OC (2004) The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid. Biochemistry 43:6159-6166. (Pubitemid 38669484)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 6159-6166
    • Dale, T.1    Sanderson, L.E.2    Uhlenbeck, O.C.3
  • 12
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • DOI 10.1126/science.1064242
    • LaRiviere FJ, Wolfson AD, Uhlenbeck OC (2001) Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294:165-168. (Pubitemid 32952970)
    • (2001) Science , vol.294 , Issue.5540 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 13
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog
    • Nissen P, et al. (1995) Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 270:1464-1472.
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1
  • 14
    • 34249074643 scopus 로고    scopus 로고
    • Exploring the specificity of bacterial elongation factor Tu for different tRNAs
    • DOI 10.1021/bi602548v
    • Sanderson LE, Uhlenbeck OC (2007) Exploring the specificity of bacterial elongation factor Tu for different tRNAs. Biochemistry 46:6194-6200. (Pubitemid 46842862)
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6194-6200
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 15
    • 34248993209 scopus 로고    scopus 로고
    • The 51-63 base pair of tRNA confers specificity for binding by EF-Tu
    • DOI 10.1261/rna.485307
    • Sanderson LE, Uhlenbeck OC (2007) The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA 13:835-840. (Pubitemid 46799817)
    • (2007) RNA , vol.13 , Issue.6 , pp. 835-840
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 16
    • 60849128493 scopus 로고    scopus 로고
    • Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis
    • Schrader JM, Chapman SJ, Uhlenbeck OC (2009) Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis. J Mol Biol 386:1255-1264.
    • (2009) J Mol Biol , vol.386 , pp. 1255-1264
    • Schrader, J.M.1    Chapman, S.J.2    Uhlenbeck, O.C.3
  • 18
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing TM, 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
  • 19
    • 0022412615 scopus 로고
    • Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes
    • DOI 10.1021/bi00344a019
    • Louie A, Jurnak F (1985) Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes. Biochemistry 24:6433-6439. (Pubitemid 16207114)
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6433-6439
    • Louie, A.1    Jurnak, F.2
  • 20
    • 0033990904 scopus 로고    scopus 로고
    • The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability
    • Vorstenbosch EL, Potapov AP, de Graaf JM, Kraal B (2000) The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability. J Biochem Biophys Methods 42:1-14.
    • (2000) J Biochem Biophys Methods , vol.42 , pp. 1-14
    • Vorstenbosch, E.L.1    Potapov, A.P.2    De Graaf, J.M.3    Kraal, B.4
  • 21
    • 0028180696 scopus 로고
    • Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation
    • Nazarenko IA, Harrington KM, Uhlenbeck OC (1994) Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation. EMBO J 13:2464-2471.
    • (1994) EMBO J , vol.13 , pp. 2464-2471
    • Nazarenko, I.A.1    Harrington, K.M.2    Uhlenbeck, O.C.3
  • 22
    • 0031777385 scopus 로고    scopus 로고
    • Recognition of the universally conserved 3′-CCA end of tRNA by elongation factor EF-Tu
    • Liu JC, LiuM, Horowitz J (1998) Recognition of the universally conserved 3′-CCA end of tRNA by elongation factor EF-Tu. RNA 4:639-646.
    • (1998) RNA , vol.4 , pp. 639-646
    • Liu, J.C.1    Liu, M.2    Horowitz, J.3
  • 23
    • 0025614348 scopus 로고
    • Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides
    • Perret V, et al. (1990) Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides. Biochimie 72:735-743.
    • (1990) Biochimie , vol.72 , pp. 735-743
    • Perret, V.1
  • 24
    • 17644366135 scopus 로고    scopus 로고
    • val
    • DOI 10.1021/bi0473399
    • Vermeulen A, McCallum SA, Pardi A (2005) Comparison of the global structure and dynamics of native and unmodified tRNAval. Biochemistry 44:6024-6033. (Pubitemid 40570696)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6024-6033
    • Vermeulen, A.1    McCallum, S.A.2    Pardi, A.3
  • 25
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson JR, Uhlenbeck OC (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
  • 26
    • 0041735420 scopus 로고    scopus 로고
    • Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome
    • DOI 10.1016/S0022-2836(03)00947-1
    • Daviter T, Wieden HJ, Rodnina MV (2003) Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome. J Mol Biol 332:689-699. (Pubitemid 37075990)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.3 , pp. 689-699
    • Daviter, T.1    Wieden, H.-J.2    Rodnina, M.V.3
  • 27
    • 46149104347 scopus 로고    scopus 로고
    • Different aa-tRNAs Are Selected Uniformly on the Ribosome
    • DOI 10.1016/j.molcel.2008.04.026, PII S1097276508003353
    • Ledoux S, Uhlenbeck OC (2008) Different aa-tRNAs are selected uniformly on the ribosome. Mol Cell 31:114-123. (Pubitemid 351905919)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 114-123
    • Ledoux, S.1    Uhlenbeck, O.C.2
  • 28
    • 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 Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J 17:7490-7497. (Pubitemid 29002715)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 29
    • 0029006133 scopus 로고
    • Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome
    • Rodnina MV, Fricke R, Kuhn L, Wintermeyer W (1995) Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome. EMBO J 14:2613-2619.
    • (1995) EMBO J , vol.14 , pp. 2613-2619
    • Rodnina, M.V.1    Fricke, R.2    Kuhn, L.3    Wintermeyer, W.4
  • 30
    • 18844408328 scopus 로고    scopus 로고
    • An active role for tRNA in decoding beyond codon:anticodon pairing
    • DOI 10.1126/science.1111408
    • Cochella L, Green R (2005) An active role for tRNA in decoding beyond codon: anticodon pairing. Science 308:1178-1180. (Pubitemid 40696436)
    • (2005) Science , vol.308 , Issue.5725 , pp. 1178-1180
    • Cochella, L.1    Green, R.2
  • 32
    • 58549114677 scopus 로고    scopus 로고
    • Slow peptide bond formation by proline and other N-alkylamino acids in translation
    • Pavlov MY, et al. (2009) Slow peptide bond formation by proline and other N-alkylamino acids in translation. Proc Natl Acad Sci USA 106:50-54.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 50-54
    • Pavlov, M.Y.1
  • 33
    • 38649088907 scopus 로고    scopus 로고
    • 32P]-labeling tRNA with nucleotidyltransferase for assaying aminoacylation and peptide bond formation
    • DOI 10.1016/j.ymeth.2007.08.001, PII S1046202307001417
    • Ledoux S, Uhlenbeck OC (2008) [3′-32P]-labeling tRNA with nucleotidyltransferase for assaying aminoacylation and peptide bond formation. Methods 44:74-80. (Pubitemid 351172805)
    • (2008) Methods , vol.44 , Issue.2 , pp. 74-80
    • Ledoux, S.1    Uhlenbeck, O.C.2
  • 34
  • 35
    • 0344026255 scopus 로고    scopus 로고
    • Single atom modification (O → S) of tRNA confers ribosome binding
    • Ashraf SS, et al. (1999) Single atom modification (O → S) of tRNA confers ribosome binding. RNA 5:188-194.
    • (1999) RNA , vol.5 , pp. 188-194
    • Ashraf, S.S.1
  • 36
    • 78651083730 scopus 로고    scopus 로고
    • PH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA
    • Johansson M, et al. (2010) pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA. Proc Natl Acad Sci USA 108:79-84.
    • (2010) Proc Natl Acad Sci USA , vol.108 , pp. 79-84
    • Johansson, M.1
  • 37
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou YM, Schimmel P (1988) A simple structural feature is a major determinant of the identity of a transfer RNA. Nature 333:140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.M.1    Schimmel, P.2
  • 38
    • 0025098898 scopus 로고
    • Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study
    • Dell VA, Miller DL, Johnson AE (1990) Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study. Biochemistry 29:1757-1763. (Pubitemid 20074718)
    • (1990) Biochemistry , vol.29 , Issue.7 , pp. 1757-1763
    • Dell, V.A.1    Miller, D.L.2    Johnson, A.E.3
  • 39
    • 34247376550 scopus 로고    scopus 로고
    • Anticodon-dependent conservation of bacterial tRNA gene sequences
    • DOI 10.1261/rna.345907
    • Saks ME, Conery JS (2007) Anticodon-dependent conservation of bacterial tRNA gene sequences. RNA 13:651-660. (Pubitemid 46641523)
    • (2007) RNA , vol.13 , Issue.5 , pp. 651-660
    • Saks, M.E.1    Conery, J.S.2
  • 40
    • 79955079756 scopus 로고    scopus 로고
    • The specific interaction between aminoacyltRNAs and elongation factor Tu
    • eds M Rodnina, R Green, and W Wintermeyer (Springer, NewYork), in press
    • Schrader J, Saks M, Uhlenbeck OC (2011) The specific interaction between aminoacyltRNAs and elongation factor Tu. Ribosomes: Structure, Function & Dynamics, eds M Rodnina, R Green, and W Wintermeyer (Springer, NewYork), in press.
    • (2011) Ribosomes: Structure, Function & Dynamics
    • Schrader, J.1    Saks, M.2    Uhlenbeck, O.C.3
  • 41
    • 70449597245 scopus 로고    scopus 로고
    • Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
    • Guo J, Melancon CE, III, Lee HS, Groff D, Schultz PG (2009) Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids. Angew Chem Int Ed Engl 48:9148-9151.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 9148-9151
    • Guo, J.1    Melancon III, C.E.2    Lee, H.S.3    Groff, D.4    Schultz, P.G.5
  • 42
    • 29244487058 scopus 로고    scopus 로고
    • Binding efficiency of elongation factor Tu to tRNAs charged with nonnatural fluorescent amino acids
    • DOI 10.1016/j.ab.2005.08.008, PII S0003269705005890
    • Nakata H, Ohtsuki T, Abe R, Hohsaka T, Sisido M (2006) Binding efficiency of elongation factor Tu to tRNAs charged with nonnatural fluorescent amino acids. Anal Biochem 348:321-323. (Pubitemid 41832538)
    • (2006) Analytical Biochemistry , vol.348 , Issue.2 , pp. 321-323
    • Nakata, H.1    Ohtsuki, T.2    Abe, R.3    Hohsaka, T.4    Sisido, M.5
  • 43
    • 77449117999 scopus 로고    scopus 로고
    • Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelB
    • Paleskava A, Konevega AL, Rodnina MV (2010) Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelB. J Biol Chem 285:3014-3020.
    • (2010) J Biol Chem , vol.285 , pp. 3014-3020
    • Paleskava, A.1    Konevega, A.L.2    Rodnina, M.V.3
  • 44
    • 0025737972 scopus 로고
    • A functional pseudoknot in 16S ribosomal RNA
    • Powers T, Noller HF (1991) A functional pseudoknot in 16S ribosomal RNA. EMBO J 10:2203-2214. (Pubitemid 21905693)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2
  • 45
    • 9744230656 scopus 로고    scopus 로고
    • Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites
    • DOI 10.1016/j.molcel.2004.10.030, PII S1097276504006550
    • Fahlman RP, Dale T, Uhlenbeck OC (2004) Uniform binding of aminoacylated transfer RNAs to the ribosomal A and P sites. Mol Cell 16:799-805. (Pubitemid 39586537)
    • (2004) Molecular Cell , vol.16 , Issue.5 , pp. 799-805
    • Fahlman, R.P.1    Dale, T.2    Uhlenbeck, O.C.3
  • 46
    • 33947324018 scopus 로고    scopus 로고
    • Phe
    • DOI 10.1016/j.jmb.2007.01.075, PII S0022283607001404
    • Sanderson LE, Uhlenbeck OC (2007) Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNA(Phe). J Mol Biol 368:119-130. (Pubitemid 46441218)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 119-130
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 47
    • 34047143747 scopus 로고    scopus 로고
    • Automated parallel isolation of multiple species of non-coding RNAs by the reciprocal circulating chromatography method
    • Miyauchi K, Ohara T, Suzuki T (2007) Automated parallel isolation of multiple species of non-coding RNAs by the reciprocal circulating chromatography method. Nucleic Acids Res 35:e24.
    • (2007) Nucleic Acids Res , vol.35
    • Miyauchi, K.1    Ohara, T.2    Suzuki, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.