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Volumn 287, Issue 24, 2012, Pages 20382-20394

Riboswitch (T-box)-mediated control of tRNA-dependent amidation in Clostridium acetobutylicum rationalizes gene and pathway redundancy for asparagine and asparaginyl-tRNAAsn synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ACIDOGENESIS; AMIDATION; CLOSTRIDIUM ACETOBUTYLICUM; GENETIC APPROACH; RIBOSWITCHES; SIMULTANEOUS USE; SOLVENTOGENESIS; SYNTHETASES; TRANSAMIDATION;

EID: 84862015362     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.332304     Document Type: Article
Times cited : (20)

References (53)
  • 1
    • 41849117355 scopus 로고    scopus 로고
    • From one amino acid to another: tRNA-dependent amino acid biosynthesis
    • DOI 10.1093/nar/gkn015
    • Sheppard, K., Yuan, J., Hohn, M. J., Jester, B., Devine, K. M., and Söll, D. (2008) From one amino acid to another: tRNA-dependent amino acid biosynthesis. Nucleic Acids Res. 36, 1813-1825 (Pubitemid 351494228)
    • (2008) Nucleic Acids Research , vol.36 , Issue.6 , pp. 1813-1825
    • Sheppard, K.1    Yuan, J.2    Hohn, M.J.3    Jester, B.4    Devine, K.M.5    Soll, D.6
  • 2
    • 0030811296 scopus 로고    scopus 로고
    • Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes
    • DOI 10.1021/bi970392v
    • Becker, H. D., Reinbolt, J., Kreutzer, R., Giegé, R., and Kern, D. (1997) Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes. Biochemistry 36, 8785-8797 (Pubitemid 27342524)
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8785-8797
    • Becker, H.D.1    Reinbolt, J.2    Kreutzer, R.3    Giege, R.4    Kern, D.5
  • 3
    • 0030613553 scopus 로고    scopus 로고
    • Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
    • Curnow, A. W., Hong, K., Yuan, R., Kim, S., Martins, O., Winkler, W., Henkin, T. M., and Söll, D. (1997) Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proc. Natl. Acad. Sci. U.S.A. 94, 11819-11826
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11819-11826
    • Curnow, A.W.1    Hong, K.2    Yuan, R.3    Kim, S.4    Martins, O.5    Winkler, W.6    Henkin, T.M.7    Söll, D.8
  • 5
    • 0034617450 scopus 로고    scopus 로고
    • The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln)
    • DOI 10.1016/S0014-5793(00)01697-5, PII S0014579300016975
    • Becker, H. D., Min, B., Jacobi, C., Raczniak, G., Pelaschier, J., Roy, H., Klein, S., Kern, D., and Söll, D. (2000) The heterotrimeric Thermus thermophilus Asp-tRNAAsn amidotransferase can also generate Gln-tRNAGln. FEBS Lett. 476, 140-144 (Pubitemid 30410805)
    • (2000) FEBS Letters , vol.476 , Issue.3 , pp. 140-144
    • Becker, H.D.1    Min, B.2    Jacobi, C.3    Raczniak, G.4    Pelaschier, J.5    Roy, H.6    Klein, S.7    Kern, D.8    Soll, D.9
  • 6
    • 0034618571 scopus 로고    scopus 로고
    • Domain-specific recruitment of amide amino acids for protein synthesis
    • Tumbula, D. L., Becker, H. D., Chang, W. Z., and Söll, D. (2000) Domain-specific recruitment of amide amino acids for protein synthesis. Nature 407, 106-110
    • (2000) Nature , vol.407 , pp. 106-110
    • Tumbula, D.L.1    Becker, H.D.2    Chang, W.Z.3    Söll, D.4
  • 8
    • 0034724203 scopus 로고    scopus 로고
    • Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase
    • DOI 10.1021/bi992573y
    • Becker, H. D., Roy, H., Moulinier, L., Mazauric, M. H., Keith, G., and Kern, D. (2000) Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase. Biochemistry 39, 3216-3230 (Pubitemid 30169990)
    • (2000) Biochemistry , vol.39 , Issue.12 , pp. 3216-3230
    • Becker, H.D.1    Roy, H.2    Moulinier, L.3    Mazauric, M.-H.4    Keith, G.5    Kern, D.6
  • 9
    • 0025017824 scopus 로고
    • Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species
    • Lévêque, F., Plateau, P., Dessen, P., and Blanquet, S. (1990) Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species. Nucleic Acids Res. 18, 305-312
    • (1990) Nucleic Acids Res. , vol.18 , pp. 305-312
    • Lévêque, F.1    Plateau, P.2    Dessen, P.3    Blanquet, S.4
  • 10
    • 0028951718 scopus 로고
    • The occurrence of duplicate lysyl-tRNA synthetase gene homologs in Escherichia coli and other procaryotes
    • Saluta, M. V., and Hirshfield, I. N. (1995) The occurrence of duplicate lysyl-tRNA synthetase gene homologs in Escherichia coli and other procaryotes. J. Bacteriol. 177, 1872-1878
    • (1995) J. Bacteriol. , vol.177 , pp. 1872-1878
    • Saluta, M.V.1    Hirshfield, I.N.2
  • 12
    • 73349114657 scopus 로고    scopus 로고
    • Recognition of tRNAGln by Helicobacter pylori GluRS2-a tRNAGln-specific glutamyl-tRNA synthetase
    • Chang, K. M., and Hendrickson, T. L. (2009) Recognition of tRNAGln by Helicobacter pylori GluRS2-a tRNAGln-specific glutamyl-tRNA synthetase. Nucleic Acids Res. 37, 6942-6949
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6942-6949
    • Chang, K.M.1    Hendrickson, T.L.2
  • 14
    • 0030901060 scopus 로고    scopus 로고
    • Specificity of tRNA-mRNA interactions in Bacillus subtilis tyrS antitermination
    • Grundy, F. J., Hodil, S. E., Rollins, S. M., and Henkin, T. M. (1997) Specificity of tRNA-mRNA interactions in Bacillus subtilis tyrS antitermination. J. Bacteriol. 179, 2587-2594 (Pubitemid 27164558)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2587-2594
    • Grundy, F.J.1    Hodil, S.E.2    Rollins, S.M.3    Henkin, T.M.4
  • 15
    • 48649110623 scopus 로고    scopus 로고
    • An in silico analysis of T-box regulated genes and T-box evolution in prokaryotes, with emphasis on prediction of substrate specificity of transporters
    • Wels, M., Groot Kormelink, T., Kleerebezem, M., Siezen, R. J., and Francke, C. (2008) An in silico analysis of T-box regulated genes and T-box evolution in prokaryotes, with emphasis on prediction of substrate specificity of transporters. BMC Genomics 9, 330
    • (2008) BMC Genomics , vol.9 , pp. 330
    • Wels, M.1    Groot Kormelink, T.2    Kleerebezem, M.3    Siezen, R.J.4    Francke, C.5
  • 17
    • 0026504685 scopus 로고
    • Analysis of the Bacillus subtilis tyrS gene: Conservation of a regulatory sequence in multiple tRNA synthetase genes
    • Henkin, T. M., Glass, B. L., and Grundy, F. J. (1992) Analysis of the Bacillus subtilis tyrS gene: conservation of a regulatory sequence in multiple tRNA synthetase genes. J. Bacteriol. 174, 1299-1306
    • (1992) J. Bacteriol. , vol.174 , pp. 1299-1306
    • Henkin, T.M.1    Glass, B.L.2    Grundy, F.J.3
  • 19
    • 33745613531 scopus 로고    scopus 로고
    • tRNA regulation of gene expression: Interactions of an mRNA 5′-UTR with a regulatory tRNA
    • DOI 10.1261/rna.29906
    • Nelson, A. R., Henkin, T. M., and Agris, P. F. (2006) tRNA regulation of gene expression: interactions of an mRNA 5′-UTR with a regulatory tRNA. RNA 12, 1254-1261 (Pubitemid 43990550)
    • (2006) RNA , vol.12 , Issue.7 , pp. 1254-1261
    • Nelson, A.R.1    Henkin, T.M.2    Agris, P.F.3
  • 20
    • 84862025737 scopus 로고    scopus 로고
    • August 19, U. S. Patent 7,413,856
    • Henkin, T. M., and Grundy, F. J. (August 19, 2008) U. S. Patent 7,413,856
    • (2008)
    • Henkin, T.M.1    Grundy, F.J.2
  • 22
    • 0029893768 scopus 로고    scopus 로고
    • Identity of prokaryotic and eukaryotic tRNAAsp for aminoacylation by aspartyl-tRNA synthetase from Thermus thermophilus
    • Becker, H. D., Giegé, R., and Kern, D. (1996) Identity of prokaryotic and eukaryotic tRNAAsp for aminoacylation by aspartyl-tRNA synthetase from Thermus thermophilus. Biochemistry 35, 7447-7458
    • (1996) Biochemistry , vol.35 , pp. 7447-7458
    • Becker, H.D.1    Giegé, R.2    Kern, D.3
  • 23
    • 0032566634 scopus 로고    scopus 로고
    • Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: Production and activity
    • DOI 10.1016/S0014-5793(98)01096-5, PII S0014579398010965
    • Fechter, P., Rudinger, J., Giegé, R., and Théobald- Dietrich, A. (1998) Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity. FEBS Lett. 436, 99-103 (Pubitemid 28454614)
    • (1998) FEBS Letters , vol.436 , Issue.1 , pp. 99-103
    • Fechter, P.1    Rudinger, J.2    Giege, R.3    Theobald-Dietrich, A.4
  • 24
    • 34250843749 scopus 로고    scopus 로고
    • Structural elements defining elongation factor Tu mediated suppression of codon ambiguity
    • DOI 10.1093/nar/gkm211
    • Roy, H., Becker, H. D., Mazauric, M. H., and Kern, D. (2007) Structural elements defining elongation factor Tu mediated suppression of codon ambiguity. Nucleic Acids Res. 35, 3420-3430 (Pubitemid 47078740)
    • (2007) Nucleic Acids Research , vol.35 , Issue.10 , pp. 3420-3430
    • Roy, H.1    Becker, H.D.2    Mazauric, M.-H.3    Kern, D.4
  • 25
    • 2342587365 scopus 로고    scopus 로고
    • Characterization and Development of Two Reporter Gene Systems for Clostridium acetobutylicum
    • DOI 10.1128/AEM.70.2.798-803.2004
    • Feustel, L., Nakotte, S., and Dürre, P. (2004) Characterization and development of two reporter gene systems for Clostridium acetobutylicum. Appl. Environ. Microbiol. 70, 798-803 (Pubitemid 38568201)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.2 , pp. 798-803
    • Feustel, L.1    Nakotte, S.2    Durre, P.3
  • 26
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan, J. F., Groebe, D. R., Witherell, G. W., and Uhlenbeck, O. C. (1987) Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res. 15, 8783-8798
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 27
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • DOI 10.1016/0076-6879(89)80091-6
    • Milligan, J. F., and Uhlenbeck, O. C. (1989) Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol. 180, 51-62 (Pubitemid 20039565)
    • (1989) Methods in Enzymology , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 28
    • 38649105167 scopus 로고    scopus 로고
    • Asn
    • DOI 10.1016/j.ymeth.2007.11.012, PII S1046202307002204
    • Bailly, M., Blaise, M., Roy, H., Deniziak, M., Lorber, B., Birck, C., Becker, H. D., and Kern, D. (2008) tRNA-dependent asparagine formation in prokaryotes: characterization, isolation and structural and functional analysis of a ribonucleoprotein particle generating Asn-tRNAAsn. Methods 44, 146-163 (Pubitemid 351172815)
    • (2008) Methods , vol.44 , Issue.2 , pp. 146-163
    • Bailly, M.1    Blaise, M.2    Roy, H.3    Deniziak, M.4    Lorber, B.5    Birck, C.6    Becker, H.D.7    Kern, D.8
  • 29
    • 0028020630 scopus 로고
    • Determination of intrinsic transcription termination efficiency by RNA polymerase elongation rate
    • McDowell, J. C., Roberts, J. W., Jin, D. J., and Gross, C. (1994) Determination of intrinsic transcription termination efficiency by RNA polymerase elongation rate. Science 266, 822-825 (Pubitemid 24359295)
    • (1994) Science , vol.266 , Issue.5186 , pp. 822-825
    • McDowell, J.C.1    Roberts, J.W.2    Jin, D.J.3    Gross, C.4
  • 30
    • 65649105039 scopus 로고    scopus 로고
    • Analysis of tRNA-directed transcription antitermination in the T box system in vivo
    • Henkin, T. M. (2009) Analysis of tRNA-directed transcription antitermination in the T box system in vivo. Methods Mol. Biol. 540, 281-290
    • (2009) Methods Mol. Biol. , vol.540 , pp. 281-290
    • Henkin, T.M.1
  • 31
    • 0036208358 scopus 로고    scopus 로고
    • Control of butanol formation in Clostridium acetobutylicum by transcriptional activation
    • DOI 10.1128/JB.184.7.1966-1973.2002
    • Thormann, K., Feustel, L., Lorenz, K., Nakotte, S., and Dürre, P. (2002) Control of butanol formation in Clostridium acetobutylicum by transcriptional activation. J. Bacteriol. 184, 1966-1973 (Pubitemid 34275541)
    • (2002) Journal of Bacteriology , vol.184 , Issue.7 , pp. 1966-1973
    • Thormann, K.1    Feustel, L.2    Lorenz, K.3    Nakotte, S.4    Durre, P.5
  • 32
    • 0022066470 scopus 로고
    • The effect of pH on nitrogen supply, cell lysis, and solvent production in fermentations of Clostridium acetobutylicum
    • DOI 10.1002/bit.260270518
    • Roos, J. W., McLaughlin, J. K., and Papoutsakis, E. T. (1985) The effect of pH on nitrogen supply, cell lysis, and solvent production in fermentations of Clostridium acetobutylicum. Biotechnol. Bioeng. 27, 681-694 (Pubitemid 15121249)
    • (1985) Biotechnology and Bioengineering , vol.27 , Issue.5 , pp. 681-694
    • Roos, J.W.1    McLaughlin, J.K.2    Papoutsakis, E.T.3
  • 33
    • 0000225313 scopus 로고
    • Gerhardt, P., R. Murray, G. E., Wood, W. A., and Krieg N. R., eds American Society for Microbiology, Washington, D. C.
    • Johnson, J. L. (1994) in Methods for General and Molecular Bacteriology (Gerhardt, P., R. Murray, G. E., Wood, W. A., and Krieg N. R., eds) pp. 655-682, American Society for Microbiology, Washington, D. C.
    • (1994) Methods for General and Molecular Bacteriology , pp. 655-682
    • Johnson, J.L.1
  • 34
  • 35
    • 65449172879 scopus 로고    scopus 로고
    • Yeast mitochondrial Gln-tRNAGln is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS
    • Frechin, M., Senger, B., Brayé, M., Kern, D., Martin, R. P., and Becker, H. D. (2009) Yeast mitochondrial Gln-tRNAGln is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev. 23, 1119-1130
    • (2009) Genes Dev. , vol.23 , pp. 1119-1130
    • Frechin, M.1    Senger, B.2    Brayé, M.3    Kern, D.4    Martin, R.P.5    Becker, H.D.6
  • 36
    • 33845632933 scopus 로고    scopus 로고
    • A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine
    • DOI 10.1093/nar/gkl622
    • Bailly, M., Giannouli, S., Blaise, M., Stathopoulos, C., Kern, D., and Becker, H. D. (2006) A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine. Nucleic Acids Res. 34, 6083-6094 (Pubitemid 44942730)
    • (2006) Nucleic Acids Research , vol.34 , Issue.21 , pp. 6083-6094
    • Bailly, M.1    Giannouli, S.2    Blaise, M.3    Stathopoulos, C.4    Kern, D.5    Becker, H.D.6
  • 38
    • 34548124567 scopus 로고    scopus 로고
    • The ClosTron: A universal gene knock-out system for the genus Clostridium
    • DOI 10.1016/j.mimet.2007.05.021, PII S0167701207002084
    • Heap, J. T., Pennington, O. J., Cartman, S. T., Carter, G. P., and Minton, N. P. (2007) The ClosTron: a universal gene knock-out system for the genus Clostridium. J. Microbiol. Methods 70, 452-464 (Pubitemid 47302149)
    • (2007) Journal of Microbiological Methods , vol.70 , Issue.3 , pp. 452-464
    • Heap, J.T.1    Pennington, O.J.2    Cartman, S.T.3    Carter, G.P.4    Minton, N.P.5
  • 39
    • 41349120749 scopus 로고    scopus 로고
    • Fermentative butanol production: Bulk chemical and biofuel
    • Dürre, P. (2008) Fermentative butanol production: bulk chemical and biofuel. Ann. N.Y. Acad. Sci. 1125, 353-362
    • (2008) Ann. N.Y. Acad. Sci. , vol.1125 , pp. 353-362
    • Dürre, P.1
  • 40
    • 0026494903 scopus 로고
    • Physiological events in Clostridium acetobutylicum during the shift from acidogenesis to solventogenesis in continuous culture and presentation of a model for shift induction
    • Grupe, H., and Gottschalk, G. (1992) Physiological events in Clostridium acetobutylicum during the shift from acidogenesis to solventogenesis in continuous culture and presentation of a model for shift induction. Appl. Environ. Microbiol. 58, 3896-3902
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3896-3902
    • Grupe, H.1    Gottschalk, G.2
  • 41
    • 0033534161 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli Asparagine Synthetase B: A short journey from substrate to product
    • Larsen, T. M., Boehlein, S. K., Schuster, S. M., Richards, N. G., Thoden, J. B., Holden, H. M., and Rayment, I. (1999) Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38, 16146-16157 (Pubitemid 129520535)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16146-16157
    • Larsen, T.M.1    Boehlein, S.K.2    Schuster, S.M.3    Richards, N.G.J.4    Thoden, J.B.5    Holden, H.M.6    Rayment, I.7
  • 42
    • 0018948232 scopus 로고
    • Mutations in two unlinked genes are required to produce asparagine auxotrophy in Escherichia coli
    • Felton, J., Michaelis, S., and Wright, A. (1980) Mutations in two unlinked genes are required to produce asparagine auxotrophy in Escherichia coli. J. Bacteriol. 142, 221-228 (Pubitemid 10037498)
    • (1980) Journal of Bacteriology , vol.142 , Issue.1 , pp. 221-228
    • Felton, J.1    Michaelis, S.2    Wright, A.3
  • 43
    • 0037050272 scopus 로고    scopus 로고
    • The nitrogen assimilation control (Nac) protein represses asnC and asnA transcription in Escherichia coli
    • DOI 10.1016/S0378-1097(01)00537-7, PII S0378109701005377
    • Poggio, S., Domeinzain, C., Osorio, A., and Camarena, L. (2002) The nitrogen assimilation control (Nac) protein represses asnC and asnA transcription in Escherichia coli. FEMS Microbiol. Lett. 206, 151-156 (Pubitemid 34117611)
    • (2002) FEMS Microbiology Letters , vol.206 , Issue.2 , pp. 151-156
    • Poggio, S.1    Domeinzain, C.2    Osorio, A.3    Camarena, L.4
  • 44
    • 77955559194 scopus 로고    scopus 로고
    • A proteomic and transcriptional view of acidogenic and solventogenic steady-state cells of Clostridium acetobutylicum in a chemostat culture
    • Janssen, H., Döring, C., Ehrenreich, A., Voigt, B., Hecker, M., Bahl, H., and Fischer, R. J. (2010) A proteomic and transcriptional view of acidogenic and solventogenic steady-state cells of Clostridium acetobutylicum in a chemostat culture. Appl. Microbiol. Biotechnol. 87, 2209-2226
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 2209-2226
    • Janssen, H.1    Döring, C.2    Ehrenreich, A.3    Voigt, B.4    Hecker, M.5    Bahl, H.6    Fischer, R.J.7
  • 45
    • 40649101442 scopus 로고    scopus 로고
    • On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE
    • Sheppard, K., and Söll, D. (2008) On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. J. Mol. Biol. 377, 831-844
    • (2008) J. Mol. Biol. , vol.377 , pp. 831-844
    • Sheppard, K.1    Söll, D.2
  • 46
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31, 3406-3415
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 48
    • 0037082440 scopus 로고    scopus 로고
    • In vitro structure-function studies of the Bacillus subtilis tyrS mRNA antiterminator: Evidence for factor-independent tRNA acceptor stem binding specificity
    • Gerdeman, M. S., Henkin, T. M., and Hines, J. V. (2002) In vitro structure-function studies of the Bacillus subtilis tyrS mRNA antiterminator: evidence for factor-independent tRNA acceptor stem binding specificity. Nucleic Acids Res. 30, 1065-1072 (Pubitemid 34679676)
    • (2002) Nucleic Acids Research , vol.30 , Issue.4 , pp. 1065-1072
    • Gerdeman, M.S.1    Henkin, T.M.2    Hines, J.V.3
  • 49
    • 0032401909 scopus 로고    scopus 로고
    • In vitro and in vivo secondary structure probing of the thrS leader in Bacillus subtilis
    • Luo, D., Condon, C., Grunberg-Manago, M., and Putzer, H. (1998) In vitro and in vivo secondary structure probing of the thrS leader in Bacillus subtilis. Nucleic Acids Res. 26, 5379-5387 (Pubitemid 28542738)
    • (1998) Nucleic Acids Research , vol.26 , Issue.23 , pp. 5379-5387
    • Luo, D.1    Condon, C.2    Grunberg-Manago, M.3    Putzer, H.4
  • 50
    • 18844412633 scopus 로고    scopus 로고
    • Gly and the Bacillus subtilis glyQS T box leader RNA
    • DOI 10.1016/j.jmb.2005.03.061, PII S0022283605003517
    • Yousef, M. R., Grundy, F. J., and Henkin, T. M. (2005) Structural transitions induced by the interaction between tRNAGly and the Bacillus subtilis glyQS T box leader RNA. J. Mol. Biol. 349, 273-287 (Pubitemid 40693749)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.2 , pp. 273-287
    • Yousef, M.R.1    Grundy, F.J.2    Henkin, T.M.3    Karn, J.4
  • 51
    • 13444288185 scopus 로고    scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • DOI 10.1093/nar/gki012
    • Sprinzl, M., and Vassilenko, K. S. (2005) Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res. 33, D139-D140 (Pubitemid 40207847)
    • (2005) Nucleic Acids Research , vol.33 , Issue.DATABASE ISS.
    • Sprinzl, M.1    Vassilenko, K.S.2
  • 52
    • 0034705342 scopus 로고    scopus 로고
    • The free yeast aspartyl-tRNA synthetase differs from the tRNAAsp-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain
    • Sauter, C., Lorber, B., Cavarelli, J., Moras, D., and Giegé, R. (2000) The free yeast aspartyl-tRNA synthetase differs from the tRNAAsp-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. J. Mol. Biol. 299, 1313-1324
    • (2000) J. Mol. Biol. , vol.299 , pp. 1313-1324
    • Sauter, C.1    Lorber, B.2    Cavarelli, J.3    Moras, D.4    Giegé, R.5
  • 53
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.