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Volumn 267, Issue 2, 2000, Pages 379-393

Sequence analysis and modular organization of threonyl-tRNA synthetase from Thermus thermophilus and its interrelation with threonyl-tRNA synthetases of other origins

Author keywords

Evolution of aminoacylation systems; Extremophiles; Thermus thermophilus; Threonyl tRNA synthetase; TRNA aminoacylation

Indexed keywords

THREONINE TRANSFER RNA LIGASE;

EID: 0033985741     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01011.x     Document Type: Article
Times cited : (4)

References (73)
  • 1
    • 0018369994 scopus 로고
    • Aminoacyl-tRNA synthetases: General features and recognition of transfer RNAs
    • 1. Schimmel, P.R. & Söll, D. (1979) Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu. Rev. Biochem. 48, 602-648.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 602-648
    • Schimmel, P.R.1    Söll, D.2
  • 2
    • 0003030232 scopus 로고
    • Transfer RNAs and aminoacyl-tRNA synthetases
    • Trachsel, H., ed., CRC Press Inc, Boca Raton, FL
    • 2. Lapointe, J. & Giegé, R. (1991) Transfer RNAs and aminoacyl-tRNA synthetases. In Translation in Eukaryotes (Trachsel, H., ed.), pp. 35-69, CRC Press Inc, Boca Raton, FL.
    • (1991) Translation in Eukaryotes , pp. 35-69
    • Lapointe, J.1    Giegé, R.2
  • 3
    • 0028139739 scopus 로고
    • Aminoacyl-tRNA synthetases from higher eukaryotes
    • 3. Kisselev, L.L. & Wolfson, A.D. (1994) Aminoacyl-tRNA synthetases from higher eukaryotes. Prog. Nucleic Acids Res. 48, 86-144.
    • (1994) Prog. Nucleic Acids Res. , vol.48 , pp. 86-144
    • Kisselev, L.L.1    Wolfson, A.D.2
  • 4
    • 0001359519 scopus 로고
    • Aminoacyl-tRNA synthetases: Occurrence, structure and function
    • Söll, D. & RajBhandary, U., eds, American Society of Microbiology, Washington, DC
    • 4. Meinnel, T., Mechulam, Y. & Blanquet, S. (1994) Aminoacyl-tRNA synthetases: occurrence, structure and function. In tRNA: Structure, Biosynthesis and Function (Söll, D. & RajBhandary, U., eds), pp. 251-292, American Society of Microbiology, Washington, DC.
    • (1994) tRNA: Structure, Biosynthesis and Function , pp. 251-292
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 5
    • 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
    • 5. Ebel, J.-P., Giegé, R., Bonnet, J., Kern, D., Befort, N., Bollack, C., Fasiolo, R, 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    Giegé, R.2    Bonnet, J.3    Kern, D.4    Befort, N.5    Bollack, C.6    Fasiolo, R.7    Gangloff, J.8    Dirheimer, G.9
  • 6
    • 0001997157 scopus 로고
    • Editing mechanisms in the aminoacylation of tRNA
    • Schimmel, P.R., Söll, D. & Abelson, J.N., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • 6. Fersht, A.R. (1979) Editing mechanisms in the aminoacylation of tRNA. In Transfer RNA: Structure, Properties and Recognition (Schimmel, P.R., Söll, D. & Abelson, J.N., eds), pp. 247-254, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1979) Transfer RNA: Structure, Properties and Recognition , pp. 247-254
    • Fersht, A.R.1
  • 7
    • 0004060232 scopus 로고
    • Mechanism of aminoacyl-tRNA synthetases: Recognition and proofreading processes
    • Schimmel, P.R., Söll, D. & Abelson, J.N., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • 7. Cramer, F., Von der Haar, F. & Igloi, G.L. (1979) Mechanism of aminoacyl-tRNA synthetases: recognition and proofreading processes. In: Transfer RNA: Structure, Properties and Recognition (Schimmel, P.R., Söll, D. & Abelson, J.N., eds), pp. 267-279, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1979) Transfer RNA: Structure, Properties and Recognition , pp. 267-279
    • Cramer, F.1    Von Der Haar, F.2    Igloi, G.L.3
  • 9
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • 9. Eriani, G., Delarue, M., Poch, O., Gangloff, J. & 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
  • 10
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
    • 10. Cusack, S., Berthet-Colominas, C., Härtlein, M., Nassar, N. & Leberman, R. (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347, 249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 11
    • 0026591001 scopus 로고
    • Structural and functional relationships between aminoacyl-tRNA synthetases
    • 11. Moras, D. (1992) Structural and functional relationships between aminoacyl-tRNA synthetases. Trends Biochem. Sci. 17, 159-164.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 159-164
    • Moras, D.1
  • 12
    • 0016744245 scopus 로고
    • Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2′-or 3′-hydroxyl group of the terminal adenosine
    • 12. 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
  • 13
    • 0001422984 scopus 로고
    • Amino acids are not all initially attached to the same position of transfer RNA molecules
    • 13. Fraser, T.H. & Rich, A. (1975) Amino acids are not all initially attached to the same position of transfer RNA molecules. Proc. Natl Acad. Sci. USA 72, 3044-3048.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 3044-3048
    • Fraser, T.H.1    Rich, A.2
  • 14
    • 0008947372 scopus 로고
    • 2′-OH versus 3′-OH specificity in tRNA aminoacylation
    • Schimmel, P.R., Söll, D. & Abelson, J.N., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • 14. Hecht, S.M. (1979) 2′-OH versus 3′-OH specificity in tRNA aminoacylation. In: Transfer RNA, Structure, Properties and Recognition (Schimmel, P.R., Söll, D. & Abelson, J.N., eds), pp. 345-360, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1979) Transfer RNA, Structure, Properties and Recognition , pp. 345-360
    • Hecht, S.M.1
  • 15
    • 0001723520 scopus 로고
    • Bacterial aminoacyl-tRNA synthetases: Genes and regulation of expression
    • Söll, D. & RajBhandary, U., eds, ASM Press, Washington, D.C.
    • 15. Putzer, H., Grunberg-Manago, M. & Springer, M. (1995) Bacterial aminoacyl-tRNA synthetases: genes and regulation of expression. In tRNA: Structure, Biosynthesis and Function (Söll, D. & RajBhandary, U., eds), pp. 293-333, ASM Press, Washington, D.C.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 293-333
    • Putzer, H.1    Grunberg-Manago, M.2    Springer, M.3
  • 16
    • 0025369743 scopus 로고
    • Independent genes for two threonyl-tRNA synthetases in Bacillus subtilis
    • 16. Putzer, H., Brakhage, A.A. & Grunberg-Manago, M. (1990) Independent genes for two threonyl-tRNA synthetases in Bacillus subtilis. J. Bacteriol. 172, 4593-4602.
    • (1990) J. Bacteriol. , vol.172 , pp. 4593-4602
    • Putzer, H.1    Brakhage, A.A.2    Grunberg-Manago, M.3
  • 17
    • 0026749687 scopus 로고
    • Coordinate expression of the two threonyl-tRNA synthetase genes in Bacillus subtilis: Control by transcriptional antitermination involving a conserved regulatory sequence
    • 17. Putzer, H., Gendron, N. & Grunberg-Manago, M. (1992) Coordinate expression of the two threonyl-tRNA synthetase genes in Bacillus subtilis: control by transcriptional antitermination involving a conserved regulatory sequence. EMBO J. 11, 3117-3127.
    • (1992) EMBO J. , vol.11 , pp. 3117-3127
    • Putzer, H.1    Gendron, N.2    Grunberg-Manago, M.3
  • 18
    • 0008893257 scopus 로고
    • Symmetrical interactions between the translational operator thrS gene and dimeric threonyl-tRNA synthetase
    • 18. Bedouelle, H. (1993) Symmetrical interactions between the translational operator thrS gene and dimeric threonyl-tRNA synthetase. J. Mol. Biol. 204, 927-938.
    • (1993) J. Mol. Biol. , vol.204 , pp. 927-938
    • Bedouelle, H.1
  • 19
    • 0027853904 scopus 로고
    • Translational regulation of the E. coli threonyl-tRNA synthetase gene: Structural and functional importance of the thrS operator domains
    • 19. Brunel, C., Romby, P., Moine, H., Caillet, J., Grunberg-Manago, M., Springer, M., Ehresmann, B. & Ehresmann, C. (1993) Translational regulation of the E. 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-Manago, M.5    Springer, M.6    Ehresmann, B.7    Ehresmann, C.8
  • 21
  • 22
    • 0029282063 scopus 로고
    • Threonyl-tRNA synthetase
    • 22. Freist, W. & Gauss, D.H. (1995) Threonyl-tRNA synthetase. Biol. Hoppe Seyler 376, 213-224.
    • (1995) Biol. Hoppe Seyler , vol.376 , pp. 213-224
    • Freist, W.1    Gauss, D.H.2
  • 23
    • 0028983874 scopus 로고
    • Thr towards Saccharomyces cerevisiae threonyl-tRNA synthetase
    • Thr towards Saccharomyces cerevisiae threonyl-tRNA synthetase. Nucleic Acids Res. 23, 2831-2836.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2831-2836
    • Nameky, N.1
  • 28
    • 0000120725 scopus 로고
    • Crystallogenesis of biological macromolecules: Facts and perspectives
    • 28. Giegé, R., Lorber, B. & Théobald-Dietrich, A. (1994) Crystallogenesis of biological macromolecules: facts and perspectives. Acta Crystallogr. D50, 339-350.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 339-350
    • Giegé, R.1    Lorber, B.2    Théobald-Dietrich, A.3
  • 29
    • 0031081750 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis: Divergent routes to a common goal
    • 29. Ibba, M., Curnow, A.M. & Söll, D. (1997) Aminoacyl-tRNA synthesis: divergent routes to a common goal. Trends Biochem. Sci. 22, 39-42.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 39-42
    • Ibba, M.1    Curnow, A.M.2    Söll, D.3
  • 30
    • 0029781454 scopus 로고    scopus 로고
    • tRNA-dependent asparagine formation
    • 30. Curnow, A.W., Ibba, M. & Söll, D. (1996) tRNA-dependent asparagine formation. Nature 382, 589-590.
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Söll, D.3
  • 33
    • 0032573150 scopus 로고    scopus 로고
    • Thermus thermophilus: A link in evolution of the tRNA-dependent amino acid amidation pathways
    • 33. Becker, H.D. & Kern, D. (1998) Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. Proc. Natl Acad. Sci. USA 95, 12832-12837.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12832-12837
    • Becker, H.D.1    Kern, D.2
  • 34
    • 0032005233 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase from Thermus thermophilus: Wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional interrelation with prokaryotic and eukaryotic glycylation systems
    • 34. Mazauric, M.-H., Keith, G., Logan, D., Kreutzer, R., Giegé, R. & Kern, D. (1998) Glycyl-tRNA synthetase from Thermus thermophilus: wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional interrelation with prokaryotic and eukaryotic glycylation systems. Eur. J. Biochem. 251, 744-757.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 744-757
    • Mazauric, M.-H.1    Keith, G.2    Logan, D.3    Kreutzer, R.4    Giegé, R.5    Kern, D.6
  • 36
    • 0015952435 scopus 로고
    • Physicochemical properties of deoxyribonucleic acid from an extreme thermophile
    • 36. Oshima, T. & Imahori, K. (1974) Physicochemical properties of deoxyribonucleic acid from an extreme thermophile. J. Biochem. 75, 179-183.
    • (1974) J. Biochem. , vol.75 , pp. 179-183
    • Oshima, T.1    Imahori, K.2
  • 37
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • 37. Tabor, S. & Richardson, C.C. (1987) DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl Acad. Sci. USA 84, 4767-4771.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 38
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • 38. Kunkel, TA. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 39. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram-quantities of protein, utilizing the principle of protein dye binding
    • 40. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram-quantities of protein, utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0018595061 scopus 로고
    • The twenty aminoacyl-tRNA synthetases from Escherichia coli. General separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities
    • 41. Kern, D. & Lapointe, J. (1979) The twenty aminoacyl-tRNA synthetases from Escherichia coli. General separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities. Biochimie 61, 1257-1272.
    • (1979) Biochimie , vol.61 , pp. 1257-1272
    • Kern, D.1    Lapointe, J.2
  • 42
    • 0023057529 scopus 로고
    • Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins
    • 42. Gribskov, M. & Burgess, R.R. (1986) Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucleic Acids Res. 14, 6745-6763.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 6745-6763
    • Gribskov, M.1    Burgess, R.R.2
  • 43
    • 0025731211 scopus 로고
    • A comparison of optimal and suboptimal RNA secondary structures predicted by free energy minimization with structures determined by phylogenetic comparison
    • 43. Zuker, M., Jaeger, J.A. & Turner, D.H. (1991) A comparison of optimal and suboptimal RNA secondary structures predicted by free energy minimization with structures determined by phylogenetic comparison. Nucleic Acids Res. 19, 2707-2714.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2707-2714
    • Zuker, M.1    Jaeger, J.A.2    Turner, D.H.3
  • 45
    • 0028353870 scopus 로고
    • Threonyl-tRNA synthetase from Thermus thermophilus: Purification and some structural and kinetic properties
    • 45. Zhelnotosova, J., Melnikova, E., Garber, M., Reinbolt, J., Kern, D., Ehresmann, C. & Ehresmann, B. (1994) Threonyl-tRNA synthetase from Thermus thermophilus: Purification and some structural and kinetic properties. Biochimie 76, 71-77.
    • (1994) Biochimie , vol.76 , pp. 71-77
    • Zhelnotosova, J.1    Melnikova, E.2    Garber, M.3    Reinbolt, J.4    Kern, D.5    Ehresmann, C.6    Ehresmann, B.7
  • 46
    • 0003017350 scopus 로고
    • The genes and genomic apparatus in extreme thermophiles
    • Brock, T.D., ed. John Wiley, New York
    • 46. Oshima, T. (1986) The genes and genomic apparatus in extreme thermophiles. In Thermophiles, General Molecular and Applied Microbiology (Brock, T.D., ed.), pp. 137-157. John Wiley, New York.
    • (1986) Thermophiles, General Molecular and Applied Microbiology , pp. 137-157
    • Oshima, T.1
  • 47
    • 0024297121 scopus 로고
    • Nucleotide sequence of Thermus thermophilus HB 8 gene coding 16S RNA
    • 47. Mursina, N.V., Vorozheykina, D.P. & Matvienko, N.I. (1988) Nucleotide sequence of Thermus thermophilus HB 8 gene coding 16S RNA. Nucleic Acids Res. 16, 8172.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8172
    • Mursina, N.V.1    Vorozheykina, D.P.2    Matvienko, N.I.3
  • 48
    • 0030038728 scopus 로고    scopus 로고
    • Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the gene and crystallization of the enzyme expressed in Escherichia coli
    • 48. Seignovert, L., Härtlein, M. & Leberman, R. (1996) Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the gene and crystallization of the enzyme expressed in Escherichia coli. Eur. J. Biochem. 239, 501-508.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 501-508
    • Seignovert, L.1    Härtlein, M.2    Leberman, R.3
  • 49
    • 0027231935 scopus 로고
    • Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implication for the structure of prokaryotic aspartyl-tRNA synthetase
    • 49. Poterszman, A., Plateau, P., Moras, D., Blanquet, S., Mazauric, M.-H., Kreutzer, R. & Kern, D. (1993) Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implication for the structure of prokaryotic aspartyl-tRNA synthetase. FEBS Lett. 325, 183-186.
    • (1993) FEBS Lett. , vol.325 , pp. 183-186
    • Poterszman, A.1    Plateau, P.2    Moras, D.3    Blanquet, S.4    Mazauric, M.-H.5    Kreutzer, R.6    Kern, D.7
  • 50
    • 0026688501 scopus 로고
    • Structure of phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli
    • 50. Kreutzer, R., Kraft, V., Bobkova, E.V., Lavrik, O.L. & Sprinzl, M. (1992) Structure of phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli. Nucleic Acids Res. 20, 4173-4178.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4173-4178
    • Kreutzer, R.1    Kraft, V.2    Bobkova, E.V.3    Lavrik, O.L.4    Sprinzl, M.5
  • 52
    • 0027237407 scopus 로고
    • Studies of the hyperthermophile Thermotoga maritima by random sequencing of DNA and genomic libraries
    • 52. Kim, C.W., Markiewicz, P., Lee, J.J., Schierle, C.F. & Miller, J.H. (1993) Studies of the hyperthermophile Thermotoga maritima by random sequencing of DNA and genomic libraries. J. Mol. Biol. 231, 960-981.
    • (1993) J. Mol. Biol. , vol.231 , pp. 960-981
    • Kim, C.W.1    Markiewicz, P.2    Lee, J.J.3    Schierle, C.F.4    Miller, J.H.5
  • 54
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • 54. Matthews, B.W. (1987) Genetic and structural analysis of the protein stability problem. Biochemistry 26, 6885-6887.
    • (1987) Biochemistry , vol.26 , pp. 6885-6887
    • Matthews, B.W.1
  • 55
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • 55. Vogt, G., Woell, S. & Argos, P. (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269, 631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 57
    • 0029091055 scopus 로고
    • Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
    • 57. Logan, D.T., Mazauric, M.-H., Kern, D. & Moras, D. (1995) Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. EMBO J. 14, 4156-4167.
    • (1995) EMBO J. , vol.14 , pp. 4156-4167
    • Logan, D.T.1    Mazauric, M.-H.2    Kern, D.3    Moras, D.4
  • 58
    • 0033548581 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    • 58. Arnez, J.G., Dock-Bregeon, A.-C. & Moras, D. (1999) Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. J. Mol. Biol. 286, 1449-1459.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1449-1459
    • Arnez, J.G.1    Dock-Bregeon, A.-C.2    Moras, D.3
  • 59
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    • 59. Arnez, J.G., Harris, D.C., Mitschler, A., Rees, B., Francklyn, C.S. & Moras, D. (1995) Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J. 14, 4143-4155.
    • (1995) EMBO J. , vol.14 , pp. 4143-4155
    • Arnez, J.G.1    Harris, D.C.2    Mitschler, A.3    Rees, B.4    Francklyn, C.S.5    Moras, D.6
  • 60
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • 60. Arnez, J.G. & 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
  • 63
    • 0025930249 scopus 로고
    • Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications
    • 63. Mirande, M. (1991) Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucleic Acid Res. Mol. Biol. 40, 95-142.
    • (1991) Prog. Nucleic Acid Res. Mol. Biol. , vol.40 , pp. 95-142
    • Mirande, M.1
  • 65
    • 0031610693 scopus 로고    scopus 로고
    • A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases
    • 65. Simos, G., Sauer, A., Fasiolo, F. & Hurt, E.C. (1998) A conserved domain within Arc1p 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.C.4
  • 66
    • 0028867140 scopus 로고
    • Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data
    • 66. Cura, V., Kern, D., Mitschler, A. & Moras, D. (1995) Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data. FEBS Lett. 374, 110-112.
    • (1995) FEBS Lett. , vol.374 , pp. 110-112
    • Cura, V.1    Kern, D.2    Mitschler, A.3    Moras, D.4
  • 67
    • 0027221150 scopus 로고
    • Chemical modification and mutagenesis studies on zinc binding of aminoacyl-tRNA synthetases
    • 67. Nureki, O., Kohno, T, Sakamoto, K., Miyaszawa, T. & 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    Miyaszawa, T.4    Yokoyama, S.5
  • 68
    • 0001163067 scopus 로고
    • Small RNA oligonucleotides substrates for specific aminoacylation
    • Söll, D. & RajBhandary, U., eds, American Society of Microbiology, Washington
    • 68. Martinis, S.A. & Schimmel, P. (1995) Small RNA oligonucleotides substrates for specific aminoacylation. tRNA: Structure, Biosynthesis and Function (Söll, D. & RajBhandary, U., eds), pp. 349-370, American Society of Microbiology, Washington.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 349-370
    • Martinis, S.A.1    Schimmel, P.2
  • 70
    • 0025633837 scopus 로고
    • Crystallographic study at 2.5 Å resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP
    • 70. Brunie, S., Zelwer, C. & Riesler, 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. 216, 411-424.
    • (1990) J. Mol. Biol. , vol.216 , pp. 411-424
    • Brunie, S.1    Zelwer, C.2    Riesler, J.-L.3
  • 71
    • 0008898843 scopus 로고    scopus 로고
    • Another bridge between kingdoms: TRNA splicing in archea and eukaryotes
    • 71. Belfort, M. & Weiner, A. (1997) Another bridge between kingdoms: tRNA splicing in archea and eukaryotes. Cell 89, 100-106.
    • (1997) Cell , vol.89 , pp. 100-106
    • Belfort, M.1    Weiner, A.2
  • 72
    • 0031587829 scopus 로고    scopus 로고
    • Archea and origin(s) of DNA replication proteins
    • 72. Edgell, D.R. & Dootlittle, W.F. (1997) Archea and origin(s) of DNA replication proteins. Cell 89, 995-998.
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Dootlittle, W.F.2
  • 73
    • 0008947720 scopus 로고    scopus 로고
    • Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus
    • 73. Becker, H.D., Reinbolt, J., Kreutzer, R., Giegé, R. & Kern, D. (1997) Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Biochemistry 72, 589-598.
    • (1997) Biochemistry , vol.72 , pp. 589-598
    • Becker, H.D.1    Reinbolt, J.2    Kreutzer, R.3    Giegé, R.4    Kern, D.5


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