메뉴 건너뛰기




Volumn 15, Issue 4, 2002, Pages 188-196

tRNA discrimination by T. thermophilus phenylalanyl-tRNA synthetase at the binding step

Author keywords

Aminoacyl tRNA synthetase; Protein nucleic acid recognition; TRNA

Indexed keywords

THERMUS; THERMUS THERMOPHILUS;

EID: 0036629822     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.575     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 0001905431 scopus 로고
    • Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Purification and properties of the crystallizing enzyme
    • Ankilova VN, Reshetnikova LS, Chernaya MM, Lavrik OI. 1988. Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Purification and properties of the crystallizing enzyme. FEBS Lett. 227: 9-13.
    • (1988) FEBS Lett. , vol.227 , pp. 9-13
    • Ankilova, V.N.1    Reshetnikova, L.S.2    Chernaya, M.M.3    Lavrik, O.I.4
  • 4
    • 0016714287 scopus 로고
    • Active site stoichiometry of L-phenylalanine: tRNA ligase from Escherichia coli K10
    • Bartmann P, Hanke T, Holler E. 1975. Active site stoichiometry of L-phenylalanine: tRNA ligase from Escherichia coli K10. J. Biol. Chem. 250: 7668-7674.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7668-7674
    • Bartmann, P.1    Hanke, T.2    Holler, E.3
  • 6
    • 0003695480 scopus 로고    scopus 로고
    • Transfer RNA recognition by aminoacyl-tRNA synthetases
    • Beuning PJ, Musier-Forsyth K. 1999. Transfer RNA recognition by aminoacyl-tRNA synthetases. Biopolymers 52: 1-28.
    • (1999) Biopolymers , vol.52 , pp. 1-28
    • Beuning, P.J.1    Musier-Forsyth, K.2
  • 7
    • 0033550073 scopus 로고    scopus 로고
    • tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase
    • Bovee ML, Yan W, Sproat BS, Francklyn CS. 1999. tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase. Biochemistry 38: 13725-13735.
    • (1999) Biochemistry , vol.38 , pp. 13725-13735
    • Bovee, M.L.1    Yan, W.2    Sproat, B.S.3    Francklyn, C.S.4
  • 8
    • 0034098420 scopus 로고    scopus 로고
    • Tertiary core rearrangements in a tight binding transfer RNA aptamer
    • Bullock TL, Sherlin LD, Perona JJ. 2000. Tertiary core rearrangements in a tight binding transfer RNA aptamer. Nat. Struct. Biol. 7: 497-504.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 497-504
    • Bullock, T.L.1    Sherlin, L.D.2    Perona, J.J.3
  • 9
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey J. 1991. Gel retardation. Meth. Enzymol. 208: 103-117.
    • (1991) Meth. Enzymol. , vol.208 , pp. 103-117
    • Carey, J.1
  • 10
    • 0015885054 scopus 로고
    • Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA-synthetase recognition and particular importance of the maximal velocity
    • Ebel JP, Giege R, Bonnet J, Kern D, Befort N, Bollack C, Fasiolo F, Gangloff J, Dirheimer G. 1973. Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA-synthetase recognition and particular importance of the maximal velocity. Biochimie 55: 547-557.
    • (1973) Biochimie , vol.55 , pp. 547-557
    • Ebel, J.P.1    Giege, R.2    Bonnet, J.3    Kern, D.4    Befort, N.5    Bollack, C.6    Fasiolo, F.7    Gangloff, J.8    Dirheimer, G.9
  • 11
    • 0033609807 scopus 로고    scopus 로고
    • Asp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs
    • Asp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs. J. Mol. Biol. 291: 761-773.
    • (1999) J. Mol. Biol. , vol.291 , pp. 761-773
    • Eriani, G.1    Gangloff, J.2
  • 13
    • 0034764075 scopus 로고    scopus 로고
    • Structure at 2.6 Å resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese
    • Fishman R, Ankilova V, Moor N, Safro M. 2001. Structure at 2.6 Å resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese. Acta Crystallogr. D57: 1534-1544.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1534-1544
    • Fishman, R.1    Ankilova, V.2    Moor, N.3    Safro, M.4
  • 14
    • 0027769983 scopus 로고
    • Triple aminoacylation specificity of a chimerized transfer RNA
    • Frugier M, Florentz C, Schimmel P, Giege R. 1993. Triple aminoacylation specificity of a chimerized transfer RNA. Biochemistry 32: 14053-14061.
    • (1993) Biochemistry , vol.32 , pp. 14053-14061
    • Frugier, M.1    Florentz, C.2    Schimmel, P.3    Giege, R.4
  • 15
    • 0030061945 scopus 로고    scopus 로고
    • Evidence that specificity of microhelix charging by a class I tRNA synthetase occurs in the transition state of catalysis
    • Gale AJ, Shi J-P, Schimmel P. 1996. Evidence that specificity of microhelix charging by a class I tRNA synthetase occurs in the transition state of catalysis. Biochemistry 35: 608-615.
    • (1996) Biochemistry , vol.35 , pp. 608-615
    • Gale, A.J.1    Shi, J.-P.2    Schimmel, P.3
  • 16
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giege R, Sissler M, Florentz C. 1998. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res. 26: 5017-5035.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giege, R.1    Sissler, M.2    Florentz, C.3
  • 17
    • 0029928937 scopus 로고    scopus 로고
    • C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase
    • Glasfeld E, Landro JA, Schimmel P. 1996. C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetase. Biochemistry 35: 4139-4145.
    • (1996) Biochemistry , vol.35 , pp. 4139-4145
    • Glasfeld, E.1    Landro, J.A.2    Schimmel, P.3
  • 19
    • 0033568665 scopus 로고    scopus 로고
    • Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis
    • Ibba M, Sever S, Prætorius-Ibba M, Söll D. 1999. Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. Nucleic Acids Res. 27: 3631-3637.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3631-3637
    • Ibba, M.1    Sever, S.2    Prætorius-Ibba, M.3    Söll, D.4
  • 21
    • 0016702758 scopus 로고
    • Stepwise tRNA recognition mechanism and its kinetic consequences
    • Knorre DG. 1975. Stepwise tRNA recognition mechanism and its kinetic consequences. FEBS Lett. 58: 50-52.
    • (1975) FEBS Lett. , vol.58 , pp. 50-52
    • Knorre, D.G.1
  • 22
    • 0017190970 scopus 로고
    • Mechanism of discrimination between cognate and non-cognate tRNAs by phenylalanyl-tRNA synthetase from yeast
    • Krauss G, Riesner D, Maass G. 1976. Mechanism of discrimination between cognate and non-cognate tRNAs by phenylalanyl-tRNA synthetase from yeast. Eur. J. Biochem. 68: 81-93.
    • (1976) Eur. J. Biochem. , vol.68 , pp. 81-93
    • Krauss, G.1    Riesner, D.2    Maass, G.3
  • 23
    • 0017403960 scopus 로고
    • Mechanism of tRNA-synthetase recognition: Role of terminal A
    • Krauss G, Riesner D, Maass G. 1977. Mechanism of tRNA-synthetase recognition: Role of terminal A. Nucleic Acids Res. 4: 2253-2262.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 2253-2262
    • Krauss, G.1    Riesner, D.2    Maass, G.3
  • 24
    • 0028971246 scopus 로고
    • Phe transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction
    • Phe transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction. Nucleic Acids Res. 23: 4598-4602.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4598-4602
    • Kreutzer, R.1    Kern, D.2    Giege, R.3    Rudinger, J.4
  • 25
    • 0031590755 scopus 로고    scopus 로고
    • Domains of phenylalanyl-tRNA synthetase from Thermus thermophilus required for aminoacylation
    • Lechler A, Kreutzer R. 1997. Domains of phenylalanyl-tRNA synthetase from Thermus thermophilus required for aminoacylation. FEBS Lett. 420: 139-142.
    • (1997) FEBS Lett. , vol.420 , pp. 139-142
    • Lechler, A.1    Kreutzer, R.2
  • 26
    • 0001359519 scopus 로고
    • Chap. 14, Söll D, RajBhandary U (eds). American Society of Microbiology: Washington DC
    • Meinnel T, Mechulam Y, Blanquet S. 1995. In tRNA: Structure, Biosynthesis and Function, Chap. 14, Söll D, RajBhandary U (eds). American Society of Microbiology: Washington DC; 251-292.
    • (1995) tRNA: Structure Biosynthesis and Function , pp. 251-292
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 30
    • 0035897140 scopus 로고    scopus 로고
    • Phe nucleotides contacting the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase by photoaffinity crosslinking
    • Phe nucleotides contacting the subunits of Thermus thermophilus phenylalanyl-tRNA synthetase by photoaffinity crosslinking. Biochim. Biophys. Acta 1518: 226-236.
    • (2001) Biochim. Biophys. Acta , vol.1518 , pp. 226-236
    • Moor, N.A.1    Ankilova, V.N.2    Lavrik, O.I.3    Favre, A.4
  • 33
    • 0029806803 scopus 로고    scopus 로고
    • Mutational analysis of a leucine heptad repeat motif in a class I aminoacyl-tRNA synthetase
    • Ohannesian DW, Hou Y-M. 1996. Mutational analysis of a leucine heptad repeat motif in a class I aminoacyl-tRNA synthetase. Biochemistry 35: 14405-14412.
    • (1996) Biochemistry , vol.35 , pp. 14405-14412
    • Ohannesian, D.W.1    Hou, Y.-M.2
  • 34
    • 0024505564 scopus 로고
    • A single base pair affects binding and catalytic parameters in the molecular recognition of a transfer RNA
    • Park SJ, Hou Y-M, Schimmel P. 1989. A single base pair affects binding and catalytic parameters in the molecular recognition of a transfer RNA. Biochemistry 28: 2740-2746.
    • (1989) Biochemistry , vol.28 , pp. 2740-2746
    • Park, S.J.1    Hou, Y.-M.2    Schimmel, P.3
  • 35
    • 0021753323 scopus 로고
    • 6-ethanoadenosine into the 3′ terminus of tRNA using T4 RNA ligase
    • 6-ethanoadenosine into the 3′ terminus of tRNA using T4 RNA ligase. Eur. J. Biochem. 138: 117-123.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 117-123
    • Paulsen, H.1    Wintermeyer, W.2
  • 36
    • 0026729421 scopus 로고
    • Effect of conformational features on the aminoacylation of tRNAs and consequences on the permutation of tRNA specificities
    • Perret V, Florentz C, Puglisi JD, Giege R. 1992. Effect of conformational features on the aminoacylation of tRNAs and consequences on the permutation of tRNA specificities. J. Mol. Biol. 226: 323-333.
    • (1992) J. Mol. Biol. , vol.226 , pp. 323-333
    • Perret, V.1    Florentz, C.2    Puglisi, J.D.3    Giege, R.4
  • 37
    • 0017182937 scopus 로고
    • Structural domains of transfer RNA molecules
    • Quigley GJ, Rich A. 1976. Structural domains of transfer RNA molecules. Science 194: 796-806.
    • (1976) Science , vol.194 , pp. 796-806
    • Quigley, G.J.1    Rich, A.2
  • 38
    • 0033515439 scopus 로고    scopus 로고
    • Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue
    • Reshetnikova L, Moor N, Lavrik O, Vassylyev D. 1999. Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue. J. Mol. Biol. 287: 555-568.
    • (1999) J. Mol. Biol. , vol.287 , pp. 555-568
    • Reshetnikova, L.1    Moor, N.2    Lavrik, O.3    Vassylyev, D.4
  • 39
    • 0025343455 scopus 로고
    • Role of the tertiary nucleotides in the interaction of yeast phenylalanine tRNA with its cognate synthetase
    • Sampson JR, DiRenzo AB, Behlen LS, Uhlenbeck OC. 1990. Role of the tertiary nucleotides in the interaction of yeast phenylalanine tRNA with its cognate synthetase. Biochemistry 29: 2523-2532.
    • (1990) Biochemistry , vol.29 , pp. 2523-2532
    • Sampson, J.R.1    DiRenzo, A.B.2    Behlen, L.S.3    Uhlenbeck, O.C.4
  • 43
    • 0032575261 scopus 로고    scopus 로고
    • A peculiarity of the reaction of tRNA aminoacylation catalyzed by phenylalanyl-tRNA synthetase from the extreme thermophile Thermus thermophilus
    • Stepanov VG, Moor NA, Ankilova VN, Vasil'eva IA, Sukhanova MV, Lavrik OI. 1998. A peculiarity of the reaction of tRNA aminoacylation catalyzed by phenylalanyl-tRNA synthetase from the extreme thermophile Thermus thermophilus. Biochim. Biophys. Acta 1386: 1-15.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 1-15
    • Stepanov, V.G.1    Moor, N.A.2    Ankilova, V.N.3    Vasil'eva, I.A.4    Sukhanova, M.V.5    Lavrik, O.I.6
  • 44
    • 0026482716 scopus 로고
    • Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase
    • Tinkle Peterson E, Uhlenbeck OC. 1992. Determination of recognition nucleotides for Escherichia coli phenylalanyl-tRNA synthetase. Biochemistry 31: 10380-10389.
    • (1992) Biochemistry , vol.31 , pp. 10380-10389
    • Tinkle Peterson, E.1    Uhlenbeck, O.C.2
  • 46
    • 0028128819 scopus 로고
    • In vitro selection of small RNAs that bind to Escherichia coli phenylalanyl-tRNA synthetase
    • Tinkle Peterson E, Pan T, Coleman J, Uhlenbeck OC. 1994. In vitro selection of small RNAs that bind to Escherichia coli phenylalanyl-tRNA synthetase. J. Mol. Biol. 242: 186-192.
    • (1994) J. Mol. Biol. , vol.242 , pp. 186-192
    • Tinkle Peterson, E.1    Pan, T.2    Coleman, J.3    Uhlenbeck, O.C.4
  • 48
    • 0026497842 scopus 로고
    • RNA binding assays for Tat-derived peptides: Implications for specificity
    • Weeks KM, Crothers DM. 1992. RNA binding assays for Tat-derived peptides: Implications for specificity. Biochemistry 31: 10281-10287.
    • (1992) Biochemistry , vol.31 , pp. 10281-10287
    • Weeks, K.M.1    Crothers, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.