메뉴 건너뛰기




Volumn 105, Issue 46, 2008, Pages 17748-17753

RNA-assisted catalysis in a protein enzyme: The 2′-hydroxyl of tRNAThr A76 promotes aminoacylation by threonyl-tRNA synthetase

Author keywords

Aminoacyl tRNA synthetase; Proton relay; Threonine; Transient kinetics; Translation

Indexed keywords

RNA; THREONINE TRANSFER RNA; TRANSFER RNA;

EID: 56649088287     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0804247105     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez JG, Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22:211-216.
    • (1997) Trends Biochem Sci , vol.22 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 2
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M, Soll D (2000) Aminoacyl-tRNA synthesis. Annu Rev Biochem 69:617-650.
    • (2000) Annu Rev Biochem , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 3
    • 0027165755 scopus 로고
    • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase
    • Perona JJ, Rould MA, Steitz TA (1993) Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 32:8758-8771.
    • (1993) Biochemistry , vol.32 , pp. 8758-8771
    • Perona, J.J.1    Rould, M.A.2    Steitz, T.A.3
  • 4
    • 0028084909 scopus 로고
    • The active site of yeast aspartyl-tRNA synthetase: Structural and functional aspects of the aminoacylation reaction
    • Cavarelli J, et al. (1994) The active site of yeast aspartyl-tRNA synthetase: Structural and functional aspects of the aminoacylation reaction. EMBO J 13:327-337.
    • (1994) EMBO J , vol.13 , pp. 327-337
    • Cavarelli, J.1
  • 5
    • 14844357908 scopus 로고    scopus 로고
    • A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase
    • Guth E, Connolly SH, Bovee M, Francklyn CS (2005) A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase. Biochemistry 44:3785-3794.
    • (2005) Biochemistry , vol.44 , pp. 3785-3794
    • Guth, E.1    Connolly, S.H.2    Bovee, M.3    Francklyn, C.S.4
  • 6
    • 0033617335 scopus 로고    scopus 로고
    • Tyr complex enlightens its repressor activity and reveals an essential zinc ion in the active site
    • Tyr complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97:371-381.
    • (1999) Cell , vol.97 , pp. 371-381
    • Sankaranarayanan, R.1
  • 7
    • 0033637662 scopus 로고    scopus 로고
    • Transfer RNA-mediated editing in threonyl-tRNA synthetase: The class II solution to the double discrimination problem
    • Dock-Bregeon A, et al. (2000) Transfer RNA-mediated editing in threonyl-tRNA synthetase: The class II solution to the double discrimination problem. Cell 103:877-884.
    • (2000) Cell , vol.103 , pp. 877-884
    • Dock-Bregeon, A.1
  • 8
    • 0034124849 scopus 로고    scopus 로고
    • Zinc ion-mediated amino acid discrimination by threonyl-tRNA synthetase
    • Sankaranarayanan R, et al. (2000) Zinc ion-mediated amino acid discrimination by threonyl-tRNA synthetase. Nat Struct Biol 7:461-465.
    • (2000) Nat Struct Biol , vol.7 , pp. 461-465
    • Sankaranarayanan, R.1
  • 9
    • 0038161128 scopus 로고    scopus 로고
    • Conformational movements and cooperativity upon amino acid, ATP, and tRNA binding in threonyl-tRNA synthetase
    • Torres-Larios A, et al. (2003) Conformational movements and cooperativity upon amino acid, ATP, and tRNA binding in threonyl-tRNA synthetase. J Mol Biol 331:201-211.
    • (2003) J Mol Biol , vol.331 , pp. 201-211
    • Torres-Larios, A.1
  • 10
    • 0346963227 scopus 로고    scopus 로고
    • Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase
    • Bovee ML, Pierce MA, Francklyn CS (2003) Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. Biochemistry 42:15102-15113.
    • (2003) Biochemistry , vol.42 , pp. 15102-15113
    • Bovee, M.L.1    Pierce, M.A.2    Francklyn, C.S.3
  • 11
    • 34948876353 scopus 로고    scopus 로고
    • Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype
    • Caillet J, et al. (2007) Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype. J Bacteriol 189:6839-6848.
    • (2007) J Bacteriol , vol.189 , pp. 6839-6848
    • Caillet, J.1
  • 12
    • 33847023388 scopus 로고    scopus 로고
    • Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase
    • Guth E, Francklyn CS (2007) Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Mol Cell 25:531-542.
    • (2007) Mol Cell , vol.25 , pp. 531-542
    • Guth, E.1    Francklyn, C.S.2
  • 13
    • 0035903548 scopus 로고    scopus 로고
    • The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism
    • Moulinier L, et al. (2001) The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism. EMBO J 20:5290-5301.
    • (2001) EMBO J , vol.20 , pp. 5290-5301
    • Moulinier, L.1
  • 14
    • 0021100127 scopus 로고
    • Loss of positional specificity in the aminoacylation of Escherichia coli tRNAGly
    • Ehrenfeld GM, Francis TA, Hecht SM (1983) Loss of positional specificity in the aminoacylation of Escherichia coli tRNAGly. J Biol Chem 258:11745-11750.
    • (1983) J Biol Chem , vol.258 , pp. 11745-11750
    • Ehrenfeld, G.M.1    Francis, T.A.2    Hecht, S.M.3
  • 15
    • 0021099383 scopus 로고
    • Transfer RNA pyrophosphorolysis with CTP(ATP):tRNA nucleotidyltransferase: A direct route to tRNAs modified at the 3′ terminus
    • Francis TA, Ehrenfeld GM, Gregory MR, Hecht SM (1983) Transfer RNA pyrophosphorolysis with CTP(ATP):tRNA nucleotidyltransferase: A direct route to tRNAs modified at the 3′ terminus. J Biol Chem 258:4279-4284.
    • (1983) J Biol Chem , vol.258 , pp. 4279-4284
    • Francis, T.A.1    Ehrenfeld, G.M.2    Gregory, M.R.3    Hecht, S.M.4
  • 16
    • 0016744245 scopus 로고
    • Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2′- or 3′-hydroxyl group of the terminal adenosine
    • Sprinzl M, Cramer F (1975) Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2′- or 3′-hydroxyl group of the terminal adenosine. Proc Natl Acad Sci USA 72:3049-3053.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3049-3053
    • Sprinzl, M.1    Cramer, F.2
  • 17
    • 0017383941 scopus 로고
    • On the stereochemistry of activation of phenylalanine by phenylalanyl-tRNA synthetase from baker's yeast
    • von der Haar F, Cramer F, Eckstein F, Stahl KW (1977) On the stereochemistry of activation of phenylalanine by phenylalanyl-tRNA synthetase from baker's yeast. Eur J Biochem 76:263-267.
    • (1977) Eur J Biochem , vol.76 , pp. 263-267
    • von der Haar, F.1    Cramer, F.2    Eckstein, F.3    Stahl, K.W.4
  • 18
    • 33646568156 scopus 로고    scopus 로고
    • Participation of the tRNA A76 hydroxyl groups throughout translation
    • Weinger JS, Strobel SA (2006) Participation of the tRNA A76 hydroxyl groups throughout translation. Biochemistry 45:5939-5948.
    • (2006) Biochemistry , vol.45 , pp. 5939-5948
    • Weinger, J.S.1    Strobel, S.A.2
  • 19
    • 11944264414 scopus 로고
    • Ribonuclease revisited: Catalysis via the classical general acid-base mechanism or a triester-like mechanism
    • Herschlag D (1994) Ribonuclease revisited: Catalysis via the classical general acid-base mechanism or a triester-like mechanism. J Am Chem Soc 116:11631-11635.
    • (1994) J Am Chem Soc , vol.116 , pp. 11631-11635
    • Herschlag, D.1
  • 20
    • 0027949817 scopus 로고
    • Value of general acid-base catalysis to ribonuclease A
    • Thompson JE, Raines RT (1994) Value of general acid-base catalysis to ribonuclease A. J Am Chem Soc 116:5467-5468.
    • (1994) J Am Chem Soc , vol.116 , pp. 5467-5468
    • Thompson, J.E.1    Raines, R.T.2
  • 21
    • 33646538128 scopus 로고    scopus 로고
    • Hydride transfer versus hydrogen radical transfer in thymidylate synthase
    • Hong B, et al. (2006) Hydride transfer versus hydrogen radical transfer in thymidylate synthase. J Am Chem Soc 128:5636-5637.
    • (2006) J Am Chem Soc , vol.128 , pp. 5636-5637
    • Hong, B.1
  • 22
    • 36349020969 scopus 로고    scopus 로고
    • Mechanism of proton transfer in the 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
    • Chang YH, Chuang LY, Hwang CC (2007) Mechanism of proton transfer in the 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. J Biol Chem 282:34306-34314.
    • (2007) J Biol Chem , vol.282 , pp. 34306-34314
    • Chang, Y.H.1    Chuang, L.Y.2    Hwang, C.C.3
  • 23
    • 0021093439 scopus 로고
    • Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase
    • Hennecke M, Plapp BV (1983) Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase. Biochemistry 22:3721-3728.
    • (1983) Biochemistry , vol.22 , pp. 3721-3728
    • Hennecke, M.1    Plapp, B.V.2
  • 24
    • 1542743968 scopus 로고    scopus 로고
    • Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase
    • LeBrun LA, Park DH, Ramaswamy S, Plapp BV (2004) Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase. Biochemistry 43:3014-3026.
    • (2004) Biochemistry , vol.43 , pp. 3014-3026
    • LeBrun, L.A.1    Park, D.H.2    Ramaswamy, S.3    Plapp, B.V.4
  • 26
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM (2001) Crystal structure of a SIR2 homolog-NAD complex. Cell 105:269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 27
    • 0040286134 scopus 로고    scopus 로고
    • Determination of 2′-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: A nucleotide analogue interference study
    • Vortler CS, et al. (1998) Determination of 2′-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: A nucleotide analogue interference study. RNA 4:1444-1454.
    • (1998) RNA , vol.4 , pp. 1444-1454
    • Vortler, C.S.1
  • 28
    • 0034682612 scopus 로고    scopus 로고
    • Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2′ hydroxyls using a complete tRNA molecule
    • Pleiss JA, Wolfson AD, Uhlenbeck OC (2000) Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2′ hydroxyls using a complete tRNA molecule. Biochemistry 39:8250-8258.
    • (2000) Biochemistry , vol.39 , pp. 8250-8258
    • Pleiss, J.A.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 29
    • 0017180250 scopus 로고
    • Hydrolytic action of aminoacyl-tRNA synthetases from baker's yeast: "Chemical proofreading" preventing acylation of tRNA(I1e) with misactivated valine
    • von der Haar F, Cramer F (1976) Hydrolytic action of aminoacyl-tRNA synthetases from baker's yeast: "Chemical proofreading" preventing acylation of tRNA(I1e) with misactivated valine. Biochemistry 15:4131-4138.
    • (1976) Biochemistry , vol.15 , pp. 4131-4138
    • von der Haar, F.1    Cramer, F.2
  • 30
    • 0037036357 scopus 로고    scopus 로고
    • Plasticity of recognition of the 3′ end of mischarged tRNA by class I aminoacyl-tRNA synthetases
    • Nordin BE, Schimmel P (2002) Plasticity of recognition of the 3′ end of mischarged tRNA by class I aminoacyl-tRNA synthetases. J Biol Chem 277:20510-20517.
    • (2002) J Biol Chem , vol.277 , pp. 20510-20517
    • Nordin, B.E.1    Schimmel, P.2
  • 31
    • 33846085054 scopus 로고    scopus 로고
    • Mechanism of tRNA-dependent editing in translational quality control
    • Ling J, Roy H, Ibba M (2007) Mechanism of tRNA-dependent editing in translational quality control. Proc Natl Acad Sci USA 104:72-77.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 72-77
    • Ling, J.1    Roy, H.2    Ibba, M.3
  • 32
    • 0027181643 scopus 로고
    • Contributions of 2′-hydroxyl groups of the RNA substrate to binding and catalysis by the Tetrahymena ribozyme: An energetic picture of an active site composed of RNA
    • Herschlag D, Eckstein F, Cech TR (1993) Contributions of 2′-hydroxyl groups of the RNA substrate to binding and catalysis by the Tetrahymena ribozyme: An energetic picture of an active site composed of RNA. Biochemistry 32:8299-8311.
    • (1993) Biochemistry , vol.32 , pp. 8299-8311
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 33
    • 7544220590 scopus 로고    scopus 로고
    • Substrate-assisted catalysis of peptide bond formation by the ribosome
    • Weinger JS, et al. (2004) Substrate-assisted catalysis of peptide bond formation by the ribosome. Nat Struct Mol Biol 11:1101-1106.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1101-1106
    • Weinger, J.S.1
  • 34
    • 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
    • Schmeing TM, et al. (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.
    • (2005) Mol Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1
  • 36
    • 33745048734 scopus 로고    scopus 로고
    • Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer
    • Trobro S, Aqvist J (2006) Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer. Biochemistry 45:7049-7056.
    • (2006) Biochemistry , vol.45 , pp. 7049-7056
    • Trobro, S.1    Aqvist, J.2
  • 37
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer M, Rodnina MV (2007) The ribosomal peptidyl transferase. Mol Cell 26:311-321.
    • (2007) Mol Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 38
    • 0033987612 scopus 로고    scopus 로고
    • Ribozyme-catalyzed tRNA aminoacylation
    • Lee N, et al. (2000) Ribozyme-catalyzed tRNA aminoacylation. Nat Struct Biol 7:28-33.
    • (2000) Nat Struct Biol , vol.7 , pp. 28-33
    • Lee, N.1
  • 39
    • 0017232521 scopus 로고
    • Coenzymes as fossils of an earlier metabolic state
    • White HB, III (1976) Coenzymes as fossils of an earlier metabolic state. J Mol Evol 7:101-104.
    • (1976) J Mol Evol , vol.7 , pp. 101-104
    • White III, H.B.1
  • 40
    • 35648980939 scopus 로고    scopus 로고
    • Evidence that tRNA synthetase-directed proton transfer stops mistranslation
    • Waas WF, Schimmel P (2007) Evidence that tRNA synthetase-directed proton transfer stops mistranslation. Biochemistry 46:12062-12070.
    • (2007) Biochemistry , vol.46 , pp. 12062-12070
    • Waas, W.F.1    Schimmel, P.2
  • 41
    • 38649136232 scopus 로고    scopus 로고
    • Francklyn CS, First EA, Perona JJ, Hou Y-M (2008) Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases. Methods 44:100-118.
    • Francklyn CS, First EA, Perona JJ, Hou Y-M (2008) Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases. Methods 44:100-118.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.