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Volumn 8, Issue 3, 1996, Pages 347-357

Overproduction of phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 in Escherichia coli

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EID: 0030294522     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0110     Document Type: Article
Times cited : (10)

References (49)
  • 1
    • 0023061339 scopus 로고
    • Aminoacyl-tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • 1. Schimmel, P. (1987) Aminoacyl-tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu. Rev. Biochem. 56, 125-158.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 2
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • 2. 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
  • 3
    • 0027851759 scopus 로고
    • Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: An update
    • 3. Cusack, S. (1993) Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: An update. Biochimie 75, 1077-1081.
    • (1993) Biochimie , vol.75 , pp. 1077-1081
    • Cusack, S.1
  • 4
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • 4. Rossmann, M. G., Moras, D., and Olsen, K. W. (1977) Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194-199.
    • (1977) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 5
    • 0026591001 scopus 로고
    • Structural and functional relationships between aminoacyl-tRNA synthetases
    • 5. 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
  • 6
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • 6. Cusack, S. (1995) Eleven down and nine to go. Nature Structural Biol. 2, 824-831.
    • (1995) Nature Structural Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 7
    • 0016744245 scopus 로고
    • Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2′-or 3′-hydroxyl group of the terminal adenosine
    • 7. Sprinzl, M., and 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
  • 8
    • 0001422984 scopus 로고
    • Amino acids are not initially attached to the same position on transfer RNA molecules
    • 8. Fraser, T. H., and Rich, A. (1975) Amino acids are not initially attached to the same position on 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
  • 9
    • 0027255483 scopus 로고
    • Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases
    • 9. Carter, C. W., Jr. (1993) Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Annu. Rev. Biochem. 62, 715-748.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 715-748
    • Carter C.W., Jr.1
  • 11
    • 0026005989 scopus 로고
    • Evolution of aminoacyl-tRNA synthetase quaterny structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase
    • 11. Sanni, A., Walter, P., Boulanger, Y., Ebel, J.-P., and Fasiolo, F. (1991) Evolution of aminoacyl-tRNA synthetase quaterny structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase. Proc. Natl. Acad. Sci. USA 88, 8387-8391.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8387-8391
    • Sanni, A.1    Walter, P.2    Boulanger, Y.3    Ebel, J.-P.4    Fasiolo, F.5
  • 12
    • 0027231935 scopus 로고
    • Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus: Implications for the structure of prokaryotic aspartyl-tRNA synthetases
    • 12. Poterszman, A., Plateau, P., Moras, D., Blanquet, S., Mazauric, M.-H., Kreutzer, R., and Kern, D. (1993) Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus: Implications for the structure of prokaryotic aspartyl-tRNA synthetases. 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
  • 13
    • 0026594157 scopus 로고
    • Cloning and sequence analysis of the phenylalanyl-tRNA synthetase genes (pheST) from Thermus thermophilus
    • 13. Keller, B., Kast, P., and Hennecke, H. (1992) Cloning and sequence analysis of the phenylalanyl-tRNA synthetase genes (pheST) from Thermus thermophilus. FEBS Lett. 301, 83-88.
    • (1992) FEBS Lett. , vol.301 , pp. 83-88
    • Keller, B.1    Kast, P.2    Hennecke, H.3
  • 14
    • 0026688501 scopus 로고
    • Structure of the phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli
    • 14. Kreutzer, R., Kruft, V., Bobkova, E. V., Lavrik, O. I., and Sprinzl, M. (1992) Structure of the 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    Kruft, V.2    Bobkova, E.V.3    Lavrik, O.I.4    Sprinzl, M.5
  • 15
    • 0029379602 scopus 로고
    • Overexpression and purification of Thermus thermophilus elongation factors G, Tu and Ts from Escherichia coli
    • 15. Blank, J., Grillenbeck, N. W., Kreutzer, R., and Sprinzl, M. (1995) Overexpression and purification of Thermus thermophilus elongation factors G, Tu and Ts from Escherichia coli. Protein Exp. Purif. 6, 637-645.
    • (1995) Protein Exp. Purif. , vol.6 , pp. 637-645
    • Blank, J.1    Grillenbeck, N.W.2    Kreutzer, R.3    Sprinzl, M.4
  • 18
  • 19
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • 19. Miller, J. (1972) "Experiments in Molecular Genetics," Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 23
    • 0028198562 scopus 로고
    • Overexpression of genes of an extreme thermophile, Thermus thermophilus, in Escherichia coli cells
    • 23. Ishida, M., and Oshima, T. (1994) Overexpression of genes of an extreme thermophile, Thermus thermophilus, in Escherichia coli cells. J. Bacteriol. 176, 2767-2770.
    • (1994) J. Bacteriol. , vol.176 , pp. 2767-2770
    • Ishida, M.1    Oshima, T.2
  • 24
    • 0029026251 scopus 로고
    • Screening and analysis of DNA fragments that show promoter activities in Thermus thermophilus
    • 24. Maseda, H., and Hoshino, T. (1995) Screening and analysis of DNA fragments that show promoter activities in Thermus thermophilus. FEMS Microbiol. Lett. 128, 127-134.
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 127-134
    • Maseda, H.1    Hoshino, T.2
  • 25
    • 0020649604 scopus 로고
    • The tac promoter: A functional hybrid derived from the trp and lac promoters
    • 25. de Boer, H. A., Comstock, L. J., and Vasser, M. (1983) The tac promoter: A functional hybrid derived from the trp and lac promoters. Proc. Natl. Acad. Sci. USA 80, 21-25.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 21-25
    • De Boer, H.A.1    Comstock, L.J.2    Vasser, M.3
  • 26
    • 0001030631 scopus 로고
    • Regulation of ribosomal RNA promoters with synthetic lac operator
    • 26. Brosius, J., and Holy, A. (1984) Regulation of ribosomal RNA promoters with synthetic lac operator. Proc. Natl. Acad. Sci. USA 81, 6929-6933.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6929-6933
    • Brosius, J.1    Holy, A.2
  • 27
    • 0028909719 scopus 로고
    • Onevector system for mutagenesis and overexpression of cloned genes
    • 27. Nock, S., Lechler, A., Ribeiro, S., and Kreutzer, R. (1995) Onevector system for mutagenesis and overexpression of cloned genes. BioTechniques 18, 608.
    • (1995) BioTechniques , vol.18 , pp. 608
    • Nock, S.1    Lechler, A.2    Ribeiro, S.3    Kreutzer, R.4
  • 28
    • 0019820038 scopus 로고
    • DNA sequences of the araBAD-araC controlling region in Salmonella typhimurium LT2
    • 28. Horwitz, A. H., Heffernan, L., Morandi, C., Lee, J.-H., Timko, J., and Wilcox, G. (1981) DNA sequences of the araBAD-araC controlling region in Salmonella typhimurium LT2. Gene 14, 309-319.
    • (1981) Gene , vol.14 , pp. 309-319
    • Horwitz, A.H.1    Heffernan, L.2    Morandi, C.3    Lee, J.-H.4    Timko, J.5    Wilcox, G.6
  • 29
    • 0029670027 scopus 로고    scopus 로고
    • Elongation factor Ts from Thermus thermophilus: Overproduction in E. coli, quaternary structure and interaction with elongation factor Tu
    • 29. Blank, J., Nock, S., Kreutzer, R., and Sprinzl, M. (1996) Elongation factor Ts from Thermus thermophilus: Overproduction in E. coli, quaternary structure and interaction with elongation factor Tu. Eur. J. Biochem. 236, 222-227.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 222-227
    • Blank, J.1    Nock, S.2    Kreutzer, R.3    Sprinzl, M.4
  • 30
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • (Wu, R., Grossman, L., and Moldave, K., Eds.), Academic Press, New York
    • 30. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes, in "Methods In Enzymology" (Wu, R., Grossman, L., and Moldave, K., Eds.), Vol. 185, pp. 60-89, Academic Press, New York.
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 31
    • 0021813890 scopus 로고
    • Convergently functional, Rho-independent terminator in Salmonella typhimurium
    • 31. Carlomagno, M. S., Riccio, A., and Bruni, C. B. (1985) Convergently functional, Rho-independent terminator in Salmonella typhimurium. J. Bacteriol. 163, 362-368.
    • (1985) J. Bacteriol. , vol.163 , pp. 362-368
    • Carlomagno, M.S.1    Riccio, A.2    Bruni, C.B.3
  • 32
    • 0026027218 scopus 로고
    • A consensus motif common to all Rho-dependent prokaryotic transcription terminators
    • 32. Alifano, P., Rivellini, F., Limauro, D., Bruni, C. B., and Carlomagno, M. S. (1991) A consensus motif common to all Rho-dependent prokaryotic transcription terminators. Cell 64, 553-563.
    • (1991) Cell , vol.64 , pp. 553-563
    • Alifano, P.1    Rivellini, F.2    Limauro, D.3    Bruni, C.B.4    Carlomagno, M.S.5
  • 33
    • 0017840778 scopus 로고
    • Studies on the altered Rho factor in nitA mutants of Escherichia coli defective in transcription termination. I. Characterization and quantitative determination of Rho in cell extracts
    • 33. Imai, M., and Shigesada, K. (1978) Studies on the altered Rho factor in nitA mutants of Escherichia coli defective in transcription termination. I. Characterization and quantitative determination of Rho in cell extracts. J. Mol. Biol. 120, 451-466.
    • (1978) J. Mol. Biol. , vol.120 , pp. 451-466
    • Imai, M.1    Shigesada, K.2
  • 34
    • 0026563620 scopus 로고
    • A comparative study of the relationship between thermostability and function of phenylalanyl-tRNA synthetases from Escherichia coli and Thermus thermophilus
    • 34. Bobkova, E. V., Stepanov, V. G., and Lavrik, O. I. (1992) A comparative study of the relationship between thermostability and function of phenylalanyl-tRNA synthetases from Escherichia coli and Thermus thermophilus. FEBS Lett. 302, 54-56.
    • (1992) FEBS Lett. , vol.302 , pp. 54-56
    • Bobkova, E.V.1    Stepanov, V.G.2    Lavrik, O.I.3
  • 35
    • 0001905431 scopus 로고
    • Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Purification and properties of the crystallizing enzyme
    • 35. Ankilova, V. N., Reshetnikova, L. S., Chernaya, M. M., and Lavrik, O. I. (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
  • 36
    • 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    Giegé, R.3    Rudinger, J.4
  • 38
    • 0026824909 scopus 로고
    • Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37
    • 38. Kast, P., Keller, B., and Hennecke, H. (1992) Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37. J. Bacteriol. 174, 1686-1689.
    • (1992) J. Bacteriol. , vol.174 , pp. 1686-1689
    • Kast, P.1    Keller, B.2    Hennecke, H.3
  • 39
    • 0025348395 scopus 로고
    • Suppression of the negative effect of minor arginine codons on gene expression; preferential usage of minor codons within the first 25 codons of the Escherichia coli genes
    • 39. Chen, G.-F. T., and Inouye, M. (1990) Suppression of the negative effect of minor arginine codons on gene expression; preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res. 18, 1465-1473.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1465-1473
    • Chen, G.-F.T.1    Inouye, M.2
  • 40
    • 0027960812 scopus 로고
    • Role of the AGA/AGG codons, the rarest codons in global expression in Escherichia coli
    • 40. Chen, G.-F. T., and Inouye, M. (1994) Role of the AGA/AGG codons, the rarest codons in global expression in Escherichia coli. Genes Dev. 8, 2641-2652.
    • (1994) Genes Dev. , vol.8 , pp. 2641-2652
    • Chen, G.-F.T.1    Inouye, M.2
  • 41
    • 0023395492 scopus 로고
    • Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli
    • 41. Looman, A. C., Bodlaender, J., Comstock, L. J., Eaton, D., Jhurani, P., de Boer, H. A., and van Knippenberg, P. H. (1987) Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli. EMBO J. 6, 2489-2492.
    • (1987) EMBO J. , vol.6 , pp. 2489-2492
    • Looman, A.C.1    Bodlaender, J.2    Comstock, L.J.3    Eaton, D.4    Jhurani, P.5    De Boer, H.A.6    Van Knippenberg, P.H.7
  • 42
    • 0025911806 scopus 로고
    • Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus
    • 42. Bobkova, E. V., Mashanov-Golikov, A. V., Wolfson, A., Ankilova, V. N., and Lavrik, O. I. (1991) Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus. FEBS Lett. 290, 95-98.
    • (1991) FEBS Lett. , vol.290 , pp. 95-98
    • Bobkova, E.V.1    Mashanov-Golikov, A.V.2    Wolfson, A.3    Ankilova, V.N.4    Lavrik, O.I.5
  • 43
    • 0026015417 scopus 로고
    • Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations
    • 43. Kast, P., and Hennecke, H. (1991) Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations. J. Mol. Biol. 222, 99-124.
    • (1991) J. Mol. Biol. , vol.222 , pp. 99-124
    • Kast, P.1    Hennecke, H.2
  • 44
    • 0020971317 scopus 로고
    • β-Galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast
    • (Wu, R., Grossman, L., and Moldave, K., Eds.), Academic Press, New York
    • 44. Casadaban, M. J., Martinez-Arias, A., Shapira, S. K., and Chou, J. (1983) β-Galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast, in "Methods in Enzymology" (Wu, R., Grossman, L., and Moldave, K., Eds.), Vol. 100, pp. 293-308, Academic Press, New York.
    • (1983) Methods in Enzymology , vol.100 , pp. 293-308
    • Casadaban, M.J.1    Martinez-Arias, A.2    Shapira, S.K.3    Chou, J.4
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors
    • 45. Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 46
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12
    • 46. Gottesman, S., Halpern, E., and Trisler, P. (1981) Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. J. Bacteriol 148, 265-273.
    • (1981) J. Bacteriol , vol.148 , pp. 265-273
    • Gottesman, S.1    Halpern, E.2    Trisler, P.3
  • 47
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • 47. Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 48
    • 0026806408 scopus 로고
    • IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication
    • 48. Hwang, D. S., Thöny, B., and Kornberg, A. (1992) IciA protein, a specific inhibitor of initiation of Escherichia coli chromosomal replication. J. Biol. Chem. 267, 2209-2213.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2209-2213
    • Hwang, D.S.1    Thöny, B.2    Kornberg, A.3
  • 49
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • 49. Chang, A. C. Y., and Cohen, S. N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134, 1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2


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