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Volumn 97, Issue 3, 1999, Pages 371-381

The structure of threonyl-tRNA synthetase-tRNAThr complex enlightens its repressor activity and reveals an essential zinc ion in the active site

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; SYNTHETASE; THREONINE TRANSFER RNA; TRANSFER RNA; ZINC ION;

EID: 0033617335     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80746-1     Document Type: Article
Times cited : (270)

References (48)
  • 1
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez, J.G., and 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
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 3
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)
    • Biou, V., Yaremchuk, A., Tukalo, M., and Cusack, S. (1994). The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science 263, 1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 4
    • 0027853904 scopus 로고
    • Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: Structural and functional importance of the thrS operator domains
    • Brunel, C., Romby, P., Moine, H., Caillet, J., Grunberg, M.M., Springer, M., Ehresmann, B., and Ehresmann, C. (1993). Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains. Biochimie 75, 1167-1179.
    • (1993) Biochimie , vol.75 , pp. 1167-1179
    • Brunel, C.1    Romby, P.2    Moine, H.3    Caillet, J.4    Grunberg, M.M.5    Springer, M.6    Ehresmann, B.7    Ehresmann, C.8
  • 6
    • 0025633837 scopus 로고
    • Crystallographic study at 2.5 Å resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP
    • Brunie, S., Zelwer, C., and Risler, J.-L. (1990). Crystallographic study at 2.5 Å resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP. J. Mol. Biol. 276, 411-424.
    • (1990) J. Mol. Biol. , vol.276 , pp. 411-424
    • Brunie, S.1    Zelwer, C.2    Risler, J.-L.3
  • 7
    • 0027162930 scopus 로고
    • Dissection of a class II tRNA synthetase: Determinants for minihelix recognition are tightly associated with domain for amino acid activation
    • Buechter, D.D., and Schimmel, P. (1993). Dissection of a class II tRNA synthetase: determinants for minihelix recognition are tightly associated with domain for amino acid activation. Biochemistry 32, 5267-5272.
    • (1993) Biochemistry , vol.32 , pp. 5267-5272
    • Buechter, D.D.1    Schimmel, P.2
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project No. 4). (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 10
    • 0026409452 scopus 로고
    • Structural biology of zinc
    • Christianson, D.W. (1991). Structural biology of zinc. Adv. Protein Chem. 42, 281-355.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 11
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack, S. (1995). Eleven down and nine to go. Nat. Struct. Biol. 2, 824-831.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 12
    • 0032518606 scopus 로고    scopus 로고
    • TRNA (Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase
    • Cusack, S., Yaremchuk, A., Krikliviy, I., and Tukalo, M. (1998). tRNA (Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. Structure 6, 101-108.
    • (1998) Structure , vol.6 , pp. 101-108
    • Cusack, S.1    Yaremchuk, A.2    Krikliviy, I.3    Tukalo, M.4
  • 13
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • De La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 14
    • 0027674975 scopus 로고
    • The aminoacyl-tRNA synthetase family: Modules at work
    • Delarue, M., and Moras, D. (1993). The aminoacyl-tRNA synthetase family: modules at work. Bioessays 15, 675-687.
    • (1993) Bioessays , vol.15 , pp. 675-687
    • Delarue, M.1    Moras, D.2
  • 15
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence 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 sequence 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
  • 16
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 17
    • 0017326738 scopus 로고
    • Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase
    • Fersht, A.R. (1977). Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry 16, 1025-1030.
    • (1977) Biochemistry , vol.16 , pp. 1025-1030
    • Fersht, A.R.1
  • 21
    • 0028267438 scopus 로고
    • Threonyl-tRNA synthetase from yeast. Discrimination of 19 amino acids in aminoacylation of tRNA(Thr)-C-C-A and tRNA(Thr)-C-C-A(2′NH2)
    • Freist, W., Sternbach, H., and Cramer, F. (1994). Threonyl-tRNA synthetase from yeast. Discrimination of 19 amino acids in aminoacylation of tRNA(Thr)-C-C-A and tRNA(Thr)-C-C-A(2′NH2). Eur. J. Biochem. 220, 745-752.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 745-752
    • Freist, W.1    Sternbach, H.2    Cramer, F.3
  • 22
    • 0030023881 scopus 로고    scopus 로고
    • Functional evidence for indirect recognition of G. U in tRNA(Ala) by alanyl-tRNA synthetase
    • Gabriel, K., Schneider, J., and McClain, W.H. (1996). Functional evidence for indirect recognition of G. U in tRNA(Ala) by alanyl-tRNA synthetase. Science 277, 195-197.
    • (1996) Science , vol.277 , pp. 195-197
    • Gabriel, K.1    Schneider, J.2    McClain, W.H.3
  • 23
    • 0027787803 scopus 로고
    • A counterselectable pACYC184-based lacZ alpha-complementing plasmid vector with novel multiple cloning sites; construction of chromosomal deletions in Klebsiella pneumoniae
    • Geissler, S., and Drummond, M. (1993). A counterselectable pACYC184-based lacZ alpha-complementing plasmid vector with novel multiple cloning sites; construction of chromosomal deletions in Klebsiella pneumoniae. Gene 136, 253-255.
    • (1993) Gene , vol.136 , pp. 253-255
    • Geissler, S.1    Drummond, M.2
  • 24
    • 0026545111 scopus 로고
    • The specificity of translational control switched with transfer RNA identity rules
    • Graffe, M., Dondon, J., Caillet, J., Romby, P., Ehresmann, C., Ehresmann, B., and Springer, M. (1992). The specificity of translational control switched with transfer RNA identity rules. Science 255, 994-996.
    • (1992) Science , vol.255 , pp. 994-996
    • Graffe, M.1    Dondon, J.2    Caillet, J.3    Romby, P.4    Ehresmann, C.5    Ehresmann, B.6    Springer, M.7
  • 25
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coll
    • Hamilton, C.M., Aldea, M., Washburn, B.K., Babitzke, P., and Kushner, S.R. (1989). New method for generating deletions and gene replacements in Escherichia coll. J. Bacteriol. 171, 4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 27
    • 0026795220 scopus 로고
    • Editing of errors in selection of amino acids for protein synthesis
    • Jakubowski, H., and Goldman, E. (1992). Editing of errors in selection of amino acids for protein synthesis. Microbiol. Rev. 56, 412-429.
    • (1992) Microbiol. Rev. , vol.56 , pp. 412-429
    • Jakubowski, H.1    Goldman, E.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0030585191 scopus 로고    scopus 로고
    • Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition strategy
    • Jovine, L, Oubridge, C., Avis, J.M., and Nagai, K. (1996). Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition strategy. Structure 5, 621-631.
    • (1996) Structure , vol.5 , pp. 621-631
    • Jovine, L.1    Oubridge, C.2    Avis, J.M.3    Nagai, K.4
  • 30
    • 0025269273 scopus 로고
    • Genomic organization and physical mapping of the transfer RNA genes in Escherichia coli K12
    • Komine, Y., Adachi, T., Inokuchi, H., and Ozeki, H. (1990). Genomic organization and physical mapping of the transfer RNA genes in Escherichia coli K12. J. Mol. Biol. 212, 579-598.
    • (1990) J. Mol. Biol. , vol.212 , pp. 579-598
    • Komine, Y.1    Adachi, T.2    Inokuchi, H.3    Ozeki, H.4
  • 32
    • 0028057108 scopus 로고
    • Raster3D version 2.0: A program for realistic molecular graphics
    • Merrit, E., and Murphy, M. (1994). Raster3D version 2.0: a program for realistic molecular graphics. Acta Crystallgr. D 50, 869-873.
    • (1994) Acta Crystallgr. D , vol.50 , pp. 869-873
    • Merrit, E.1    Murphy, M.2
  • 33
    • 0025635930 scopus 로고
    • Escherichia coli threonyl-tRNA synthetase and tRNA(Thr) modulate the binding of the ribosome to the translational initiation site of the thrS mRNA
    • Moine, H., Romby, P., Springer, M., Grunberg-Manago, M., Ebel, J.P., Ehresmann, B., and Ehresmann, C. (1990). Escherichia coli threonyl-tRNA synthetase and tRNA(Thr) modulate the binding of the ribosome to the translational initiation site of the thrS mRNA. J. Mol. Biol. 276, 299-310.
    • (1990) J. Mol. Biol. , vol.276 , pp. 299-310
    • Moine, H.1    Romby, P.2    Springer, M.3    Grunberg-Manago, M.4    Ebel, J.P.5    Ehresmann, B.6    Ehresmann, C.7
  • 34
    • 0026766983 scopus 로고
    • Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove
    • Musier-Forsyth, K., and Schimmel, P. (1992). Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove. Nature 357, 513-515.
    • (1992) Nature , vol.357 , pp. 513-515
    • Musier-Forsyth, K.1    Schimmel, P.2
  • 35
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B. (1991). A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comp. Chem. 72, 435-445.
    • (1991) J. Comp. Chem. , vol.72 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 36
    • 0027221150 scopus 로고
    • Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases
    • Nureki, O., Kohno, T., Sakamoto, K., Miyazawa, T., and Yokoyama, S. (1993). Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases. J. Biol. Chem. 268, 15368-15373.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15368-15373
    • Nureki, O.1    Kohno, T.2    Sakamoto, K.3    Miyazawa, T.4    Yokoyama, S.5
  • 38
    • 0023700973 scopus 로고
    • Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA
    • Park, S.J., and Schimmel, P. (1988). Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA. J. Biol. Chem. 263, 16527-16530.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16527-16530
    • Park, S.J.1    Schimmel, P.2
  • 39
    • 0026457064 scopus 로고
    • Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules
    • Romby, P., Brunel, C., Caillet, J., Springer, M., Grunberg-Manago, M., Westhof, E., Ehresmann, C., and Ehresmann, B. (1992). Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules. Nucleic Acids Res. 20, 5633-5640.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5633-5640
    • Romby, P.1    Brunel, C.2    Caillet, J.3    Springer, M.4    Grunberg-Manago, M.5    Westhof, E.6    Ehresmann, C.7    Ehresmann, B.8
  • 40
  • 44
    • 0031610693 scopus 로고    scopus 로고
    • A conserved domain within Aid p delivers tRNA to aminoacyl-tRNA synthetases
    • Simos, G., Sauer, A., Fasiolo, F., and Hurt, E.G. (1998). A conserved domain within Aid p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell 1, 235-242.
    • (1998) Mol. Cell , vol.1 , pp. 235-242
    • Simos, G.1    Sauer, A.2    Fasiolo, F.3    Hurt, E.G.4
  • 46
    • 0024454753 scopus 로고
    • TRNA-like structures and gene regulation at the translational level: A case of molecular mimicry in Escherichia coli
    • Springer, M., Graffe, M., Dondon, J., and Grunberg-Manago, M. (1989). tRNA-like structures and gene regulation at the translational level: a case of molecular mimicry in Escherichia coli. EMBO J. 8, 2417-2424.
    • (1989) EMBO J. , vol.8 , pp. 2417-2424
    • Springer, M.1    Graffe, M.2    Dondon, J.3    Grunberg-Manago, M.4
  • 47
    • 0023696299 scopus 로고
    • Tertiary structure of Escherichia coli tRNA(3Thr) in solution and interaction of this tRNA with the cognate threonyl-tRNA synthetase
    • Theobald, A., Springer, M., Grunberg-Manago, M., Ebel, J.P., and Giegé, R. (1988). Tertiary structure of Escherichia coli tRNA(3Thr) in solution and interaction of this tRNA with the cognate threonyl-tRNA synthetase. Eur. J. Biochem. 775, 511-524.
    • (1988) Eur. J. Biochem. , vol.775 , pp. 511-524
    • Theobald, A.1    Springer, M.2    Grunberg-Manago, M.3    Ebel, J.P.4    Giegé, R.5
  • 48
    • 0019844454 scopus 로고
    • Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli
    • Tsui, W.C., and Fersht, A.R. (1981). Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli. Nucleic Acids Res. 9, 4627-4637.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 4627-4637
    • Tsui, W.C.1    Fersht, A.R.2


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