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Volumn 45, Issue 22, 2006, Pages 6858-6865

Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CHEMICAL MODIFICATION; CONFORMATIONS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MUTAGENESIS;

EID: 33744947970     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052606b     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M., and Söll, D. (2000) Aminoacyl-tRNA synthesis, Annu. Rev. Biochem. 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 2
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequences motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J., and Moras, D. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequences motifs, Nature 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 3
    • 0036849261 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: Versatile players in the changing theater of translation
    • Francklyn, C., Perona, J. J., Puetz, J., and Hou, Y.-M. (2002) Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation, RNA 8, 1363-1372.
    • (2002) RNA , vol.8 , pp. 1363-1372
    • Francklyn, C.1    Perona, J.J.2    Puetz, J.3    Hou, Y.-M.4
  • 4
    • 0038662765 scopus 로고    scopus 로고
    • tRNA-dependent active-site assembly in a class I aminoacyl-tRNA synthetase
    • Sherlin, L. D., and Perona, J. J. (2003) tRNA-dependent active-site assembly in a class I aminoacyl-tRNA synthetase, Structure 11, 591-603.
    • (2003) Structure , vol.11 , pp. 591-603
    • Sherlin, L.D.1    Perona, J.J.2
  • 5
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson, J. R. (2000) Induced fit in RNA-protein recognition, Nat. Struct. Biol. 7, 834-837.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 6
    • 0030017670 scopus 로고    scopus 로고
    • A mechanism for reducing entropic cost of induced fit in protein-RNA recognition
    • Ribas de Pouplana, L., Auld, D. S., Kim, S., and Schimmel, P. (1996) A mechanism for reducing entropic cost of induced fit in protein-RNA recognition, Biochemistry 35, 8095-8102.
    • (1996) Biochemistry , vol.35 , pp. 8095-8102
    • Ribas De Pouplana, L.1    Auld, D.S.2    Kim, S.3    Schimmel, P.4
  • 7
    • 0028839740 scopus 로고
    • Reexamination of induced fit as a determinant of substrate specificity in enzymatic reactions
    • Post, C. B., and Ray, W. J., Jr. (1995) Reexamination of induced fit as a determinant of substrate specificity in enzymatic reactions, Biochemistry 34, 15881-15885.
    • (1995) Biochemistry , vol.34 , pp. 15881-15885
    • Post, C.B.1    Ray Jr., W.J.2
  • 8
    • 21244469649 scopus 로고    scopus 로고
    • Glutaminyl-tRNA synthetases
    • (Ibba, M., Francklyn, C., Cusack, S., Eds.), Landes Bioscience/Eurekah. com
    • Perona, J. J. (2004) Glutaminyl-tRNA synthetases, in The Aminoacyl-tRNA Synthetases (Ibba, M., Francklyn, C., Cusack, S., Eds.) pp 73-88, Landes Bioscience/Eurekah.com.
    • (2004) The Aminoacyl-tRNA Synthetases , pp. 73-88
    • Perona, J.J.1
  • 10
    • 0027508272 scopus 로고
    • A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase
    • Bhattacharyya, T., and Roy, S. (1993) A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase, Biochemistry 32, 9268-9273.
    • (1993) Biochemistry , vol.32 , pp. 9268-9273
    • Bhattacharyya, T.1    Roy, S.2
  • 11
    • 0031977170 scopus 로고    scopus 로고
    • A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity
    • Mandal, A. K., Bhattacharyya, A., Bhattacharyya, S., Bhattacharyya, T., and Roy, S. (1998) A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity, Protein Sci. 7, 1046-1051.
    • (1998) Protein Sci. , vol.7 , pp. 1046-1051
    • Mandal, A.K.1    Bhattacharyya, A.2    Bhattacharyya, S.3    Bhattacharyya, T.4    Roy, S.5
  • 12
    • 5144223811 scopus 로고    scopus 로고
    • Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics
    • Uter, N. T., and Perona, J. J. (2004) Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics, Proc. Natl. Acad. Sci. U.S.A. 101, 14396-14401.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14396-14401
    • Uter, N.T.1    Perona, J.J.2
  • 14
    • 0027165755 scopus 로고
    • Structural basis for transfer RNA aminoacylation by E. coli glutaminyl-tRNA synthetase
    • Perona, J. J., Rould, M. A., and Steitz, T. A. (1993) Structural basis for transfer RNA aminoacylation by E. 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
  • 17
    • 14844357908 scopus 로고    scopus 로고
    • A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase
    • Guth, E., Connolly, S. H., Bovee, M., and Francklyn, C. S. (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
  • 18
    • 21244444325 scopus 로고    scopus 로고
    • Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase
    • Uter, N. T., Gruic-Sovulj, I., and Perona, J. J. (2005) Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase, J. Biol. Chem. 280, 23966-23977.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23966-23977
    • Uter, N.T.1    Gruic-Sovulj, I.2    Perona, J.J.3
  • 21
    • 0037466332 scopus 로고    scopus 로고
    • Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants
    • Bullock, T. L., Uter, N. T., Nissan, T. A., and Perona, J. J. (2003) Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants, J. Mol. Biol. 328, 395-408.
    • (2003) J. Mol. Biol. , vol.328 , pp. 395-408
    • Bullock, T.L.1    Uter, N.T.2    Nissan, T.A.3    Perona, J.J.4
  • 22
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process
    • Woese, C. R., Olsen, G. J., Ibba, M., and Söll, D. (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process, Microbiol. Mol. Biol. Rev. 64, 202-236.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 202-236
    • Woese, C.R.1    Olsen, G.J.2    Ibba, M.3    Söll, D.4
  • 23
    • 0019321933 scopus 로고
    • Structure of the metal.nucleotide complex in the yeast phenylalanyl transfer ribonucleic acid synthetase reaction as determined with diastereomeric phosphorothioate analogs of ATP
    • Connolly, B. A., Von der Haar, F., and Eckstein, F. (1980) Structure of the metal.nucleotide complex in the yeast phenylalanyl transfer ribonucleic acid synthetase reaction as determined with diastereomeric phosphorothioate analogs of ATP, J. Biol. Chem. 255, 11301-11307.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11301-11307
    • Connolly, B.A.1    Von Der Haar, F.2    Eckstein, F.3
  • 24
    • 0020029516 scopus 로고
    • Reactions of thio analogues of adenosine 5′-triphosphate catalyzed by methionyl-tRNA synthetase from Escherichia coli and metal dependence of stereospecificity
    • Smith, L. T., and Cohn, M. (1982) Reactions of thio analogues of adenosine 5′-triphosphate catalyzed by methionyl-tRNA synthetase from Escherichia coli and metal dependence of stereospecificity, Biochemistry 21, 1530-1534.
    • (1982) Biochemistry , vol.21 , pp. 1530-1534
    • Smith, L.T.1    Cohn, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.