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Volumn 15, Issue 21, 1996, Pages 5976-5987

The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions

Author keywords

Aminoacyl tRNA synthetase; mRNA; RNA protein interaction; Translational control; tRNA like structure

Indexed keywords

THREONINE TRANSFER RNA LIGASE;

EID: 10344237522     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00984.x     Document Type: Article
Times cited : (53)

References (48)
  • 1
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    • Arnez, J.G., Harris, D.C. Mitschler, A., Rees, B., Francklyn, C.S. and 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
  • 2
    • 0024264659 scopus 로고
    • Ribonucleoprotein complexes of R17 coat protein and a translational operator analog
    • Beckett, D. and Uhlenbeck, O.C. (1988) Ribonucleoprotein complexes of R17 coat protein and a translational operator analog. J. Mol. Biol., 204, 927-938.
    • (1988) J. Mol. Biol. , vol.204 , pp. 927-938
    • Beckett, D.1    Uhlenbeck, O.C.2
  • 3
    • 0027176141 scopus 로고
    • Symmetrical interactions between the translational operator of the thrS gene and dimeric threonyl-tRNA synthetase
    • Bedouelle, H. (1993) Symmetrical interactions between the translational operator of the thrS gene and dimeric threonyl-tRNA synthetase. J. Mol. Biol., 230, 704-708.
    • (1993) J. Mol. Biol. , vol.230 , pp. 704-708
    • Bedouelle, H.1
  • 4
    • 0026794193 scopus 로고
    • The domains of the E. coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors
    • Brunel, C. et al. (1992) The domains of the E. coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors. J. Mol. Biol., 227, 621-634.
    • (1992) J. Mol. Biol. , vol.227 , pp. 621-634
    • Brunel, C.1
  • 5
    • 0027853904 scopus 로고
    • Translational regulation of the E.coli threonyl-tRNA synthetase gene: Structural and functional importance of the thrS operator domains
    • Brunel, C., Romby, P., Moine, H., Caillet, J., Grunberg-Manago, M., Springer, M., Ehresmann, B. and 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
  • 6
    • 0028846649 scopus 로고
    • Stabilised secondary structure at a ribosomal binding site enhances translational repression in E.coli
    • Brunel, C. et al. (1995) Stabilised secondary structure at a ribosomal binding site enhances translational repression in E.coli. J. Mol. Biol., 253, 277-290.
    • (1995) J. Mol. Biol. , vol.253 , pp. 277-290
    • Brunel, C.1
  • 7
    • 0030590216 scopus 로고    scopus 로고
    • Growth rate-dependent control, feedback regulation and steady-state mRNA levels of the threonyl-tRNA synthetase gene of E.coli
    • Comer, M., Dondon, J., Graffe, M., Yarchuk, O. and Springer, M. (1996) Growth rate-dependent control, feedback regulation and steady-state mRNA levels of the threonyl-tRNA synthetase gene of E.coli. J. Mol. Biol., 261, 108-124.
    • (1996) J. Mol. Biol. , vol.261 , pp. 108-124
    • Comer, M.1    Dondon, J.2    Graffe, M.3    Yarchuk, O.4    Springer, M.5
  • 8
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack, S. (1995) Eleven down and nine to go. Nature Struct. Biol., 2, 824-831.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 9
    • 0017380076 scopus 로고
    • Mapping adenines, guanines, and pyrimidines in RNA
    • Donis-Keller, H., Maxam, A.M. and Gilbert, W. (1977) Mapping adenines, guanines, and pyrimidines in RNA. Nucleic Acids Res., 4, 2527-2538.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 2527-2538
    • Donis-Keller, H.1    Maxam, A.M.2    Gilbert, W.3
  • 10
    • 10344263562 scopus 로고
    • Molecular mimicry in the translational control of E.coli threonyl-tRNA synthetase expression
    • Sarma, R.H. and Sarma, M.H. (eds), Adenine Press, Schenectady, NY
    • Ehresmann, C., Romby, P., Brunel, C., Moine, H., Caillet, J., Springer, M. and Ehresmann, B. (1994) Molecular mimicry in the translational control of E.coli threonyl-tRNA synthetase expression. In Sarma, R.H. and Sarma, M.H. (eds), Structural Biology: The State of the Art. Adenine Press, Schenectady, NY, pp. 251-264.
    • (1994) Structural Biology: The State of the Art , pp. 251-264
    • Ehresmann, C.1    Romby, P.2    Brunel, C.3    Moine, H.4    Caillet, J.5    Springer, M.6    Ehresmann, B.7
  • 11
    • 0025158208 scopus 로고
    • Partition of transfer RNA synthetases into 2 classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J. and Moras, D. (1990) Partition of transfer RNA synthetases into 2 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
  • 13
    • 0025114689 scopus 로고
    • Enzymatic aminoacylation of an eight-base-pair microhelix with histidine
    • Francklyn, C. and Schimmel, P. (1990) Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc. Natl Acad. Sci. USA, 87, 8655-8659.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8655-8659
    • Francklyn, C.1    Schimmel, P.2
  • 16
    • 0017384846 scopus 로고
    • Threonyl-transfer ribonucleic acid synthetase from E.coli: Subunit structure and genetic analysis of the stuctural gene by means of a mutated enzyme and of a specialised transducing lambda bacteriophage
    • Hennecke, H., Böck, A., Thomale, J. and Nass, G. (1977) Threonyl-transfer ribonucleic acid synthetase from E.coli: subunit structure and genetic analysis of the stuctural gene by means of a mutated enzyme and of a specialised transducing lambda bacteriophage. J. Bacteriol., 131, 943-950.
    • (1977) J. Bacteriol. , vol.131 , pp. 943-950
    • Hennecke, H.1    Böck, A.2    Thomale, J.3    Nass, G.4
  • 17
    • 1842391776 scopus 로고
    • Formation of an RNA primer for initiation of replication of ColE1 DNA by ribonuclease H
    • Itoh, T. and Tomizawa, J.I. (1980) Formation of an RNA primer for initiation of replication of ColE1 DNA by ribonuclease H. Proc. Natl Acad. Sci. USA, 77, 2450-2454.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 2450-2454
    • Itoh, T.1    Tomizawa, J.I.2
  • 19
    • 0016734742 scopus 로고
    • Equivalent and non-equivalent binding sites for tRNA on aminoacyl-tRNA synthetases
    • Krauss, G., Pingoud, A., Boehme, D., Riesner, D., Peters, F. and Maass, G. (1975) Equivalent and non-equivalent binding sites for tRNA on aminoacyl-tRNA synthetases. Eur. J. Biochem., 55, 517-529.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 517-529
    • Krauss, G.1    Pingoud, A.2    Boehme, D.3    Riesner, D.4    Peters, F.5    Maass, G.6
  • 20
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Wu, R. and Grossman, L. (eds), Academic Press, New York
    • Kunkel, T.A., Roberts, J.D. and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. In Wu, R. and Grossman, L. (eds), Recombinant DNA. Part E. Academic Press, New York, pp. 367-382.
    • (1987) Recombinant DNA. Part E , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 21
    • 0029976320 scopus 로고    scopus 로고
    • Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants
    • Li, H. and Nicholson, A.W. (1996) Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants. EMBO J., 15, 1421-1433.
    • (1996) EMBO J. , vol.15 , pp. 1421-1433
    • Li, H.1    Nicholson, A.W.2
  • 22
    • 0029091055 scopus 로고
    • Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
    • Logan, D.T., Mazauric, M.H., Kern, D. and 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
  • 24
    • 0029041327 scopus 로고
    • Cytoplasmic mRNA-protein interactions in eukaryotic gene expression
    • McCarthy, J.E.C. and Kollmus, H. (1995) Cytoplasmic mRNA-protein interactions in eukaryotic gene expression. Trends Biochem. Sci., 20, 191-197.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 191-197
    • McCarthy, J.E.C.1    Kollmus, H.2
  • 25
    • 0001359519 scopus 로고
    • Aminoacyl-tRNA synthetases: Occurrence, structure and function
    • Söll, D. and RajBhandary, U.L. (eds), ASM Press, Washington, DC
    • Meinnel, T., Mechulam, Y. and Blanquet, S. (1995) Aminoacyl-tRNA synthetases: occurrence, structure and function. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. ASM Press, Washington, DC, pp 251-292.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 251-292
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 30
    • 0017357987 scopus 로고
    • Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in E.coli
    • Neidhardt, F.C., Bloch, P.L., Pedersen, S. and Reeh, S. (1977) Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in E.coli. J. Bacteriol., 129, 378-387.
    • (1977) J. Bacteriol. , vol.129 , pp. 378-387
    • Neidhardt, F.C.1    Bloch, P.L.2    Pedersen, S.3    Reeh, S.4
  • 31
    • 0028298842 scopus 로고
    • Structure of restriction endonuclease BamHI and its relationship to EcoRI
    • Newman, M., Strzelecka, T., Dorner, L.F., Shildkraut, I. and Aggarwal, A.K. (1994) Structure of restriction endonuclease BamHI and its relationship to EcoRI. Nature, 368, 660-664.
    • (1994) Nature , vol.368 , pp. 660-664
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Shildkraut, I.4    Aggarwal, A.K.5
  • 32
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C.O. and Sauer, R.T. (1992) Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem., 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 33
    • 0028873824 scopus 로고
    • Dissecting RNA-protein interactions: RNA-RNA recognition by Rop
    • Predki, P.F., Nayak, L.M., Gottlieb, M.B.C. and Regan, L. (1995) Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell, 80, 41-50.
    • (1995) Cell , vol.80 , pp. 41-50
    • Predki, P.F.1    Nayak, L.M.2    Gottlieb, M.B.C.3    Regan, L.4
  • 34
    • 0024804759 scopus 로고
    • Absorbance melting curves of RNA
    • Puglisi, J.D. and Tinoco, I. (1989) Absorbance melting curves of RNA. Methods Enzymol., 180, 304-325.
    • (1989) Methods Enzymol. , vol.180 , pp. 304-325
    • Puglisi, J.D.1    Tinoco, I.2
  • 35
    • 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
  • 39
    • 10344264639 scopus 로고
    • Translational regulation in E.coli and bacteriophage
    • Lin, E.C.C. and Iuchi, S. (eds), R.G.Landes, Austin, TX
    • Springer, M. (1995) Translational regulation in E.coli and bacteriophage. In Lin, E.C.C. and Iuchi, S. (eds), Regulation of Gene Expression in E.coli. R.G.Landes, Austin, TX.
    • (1995) Regulation of Gene Expression in E.coli
    • Springer, M.1
  • 40
    • 0018286251 scopus 로고
    • Genetic organization of the E.coli chromosome around the structural gene for initiation factor IF3 (infC)
    • Springer, M., Graffe, M. and Grunberg-Manago, M. (1979) Genetic organization of the E.coli chromosome around the structural gene for initiation factor IF3 (infC) Mol. Gen. Genet., 169, 337-343.
    • (1979) Mol. Gen. Genet. , vol.169 , pp. 337-343
    • Springer, M.1    Graffe, M.2    Grunberg-Manago, M.3
  • 41
    • 0022251303 scopus 로고
    • Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo
    • Springer, M. et al. (1985) Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo. J. Mol. Biol., 185, 93-104.
    • (1985) J. Mol. Biol. , vol.185 , pp. 93-104
    • Springer, M.1
  • 42
    • 0022515311 scopus 로고
    • Genetic definition of the translational operator of the threonine tRNA ligase gene in Escherichia coli
    • Springer, M., Graffe, M., Butler, J.S. and Grunberg-Manago, M. (1986) Genetic definition of the translational operator of the threonine tRNA ligase gene in Escherichia coli. Proc. Natl Acad. Sci. USA, 83, 4384-4388.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4384-4388
    • Springer, M.1    Graffe, M.2    Butler, J.S.3    Grunberg-Manago, M.4
  • 43
    • 0024454753 scopus 로고
    • tRNA-like structures and gene regulation at the translational level: A case of molecular mimicry in E.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 E.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
  • 44
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
    • Taylor, J.W., Ott, J. and Eckstein, F. (1985) The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Res., 13, 8765-8785.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8765-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 46
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegard, K., Murray, J.B., Stockley, P.G., Stonehouse, N.J. and Liljas, L. (1994) Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature, 371, 623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegard, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 48
    • 0028251157 scopus 로고
    • Diverse mechanisms for regulating ribosomal protein synthesis in E.coli
    • Zengel, J.M. and Lindahl, L. (1994) Diverse mechanisms for regulating ribosomal protein synthesis in E.coli. Prog. Nucleic Acid Res. Mol. Biol., 47, 331-369.
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.47 , pp. 331-369
    • Zengel, J.M.1    Lindahl, L.2


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