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Volumn 50, Issue 13, 2011, Pages 2424-2433

Rapid steps in the glmS ribozyme catalytic pathway: Cation and ligand requirements

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS RATE; CATALYTIC PATHWAYS; CHEMICAL CATALYSIS; CLEAVAGE REACTION; DIVALENT CATION; DOWN-REGULATION; EXPERIMENTAL DESIGN; GLUCOSAMINE 6-PHOSPHATE; GRAM-POSITIVE BACTERIUM; LIGAND BINDING; LIGAND SPECIFICITY; MOLAR CONCENTRATION; MONOVALENT CATIONS; RATE LIMITING; RIBOSWITCHES; RIBOZYMES; SELF-CLEAVAGE; SITE-SPECIFIC;

EID: 79953227362     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101842u     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 27144527479 scopus 로고    scopus 로고
    • Regulation of bacterial gene expression by riboswitches
    • DOI 10.1146/annurev.micro.59.030804.121336
    • Winkler, W. C. and Breaker, R. R. (2005) Regulation of bacterial gene expression by riboswitches Annu. Rev. Microbiol. 59, 487-517 (Pubitemid 41507440)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 487-517
    • Winkler, W.C.1    Breaker, R.R.2
  • 2
    • 0037206833 scopus 로고    scopus 로고
    • Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression
    • DOI 10.1038/nature01145
    • Winkler, W., Nahvi, A., and Breaker, R. R. (2002) Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression Nature 419, 952-956 (Pubitemid 35339632)
    • (2002) Nature , vol.419 , Issue.6910 , pp. 952-956
    • Winkler, W.1    Nahvi, A.2    Breaker, R.R.3
  • 3
    • 18744396047 scopus 로고    scopus 로고
    • Sensing small molecules by nascent RNA: A mechanism to control transcription in bacteria
    • DOI 10.1016/S0092-8674(02)01134-0
    • Mironov, A. S., Gusarov, I., Rafikov, R., Lopez, L. E., Shatalin, K., Kreneva, R. A., Perumov, D. A., and Nudler, E. (2002) Sensing small molecules by nascent RNA: A mechanism to control transcription in bacteria Cell 111, 747-756 (Pubitemid 35446317)
    • (2002) Cell , vol.111 , Issue.5 , pp. 747-756
    • Mironov, A.S.1    Gusarov, I.2    Rafikov, R.3    Lopez, L.E.4    Shatalin, K.5    Kreneva, R.A.6    Perumov, D.A.7    Nudler, E.8
  • 4
    • 0346687595 scopus 로고    scopus 로고
    • The riboswitch control of bacterial metabolism
    • DOI 10.1016/j.tibs.2003.11.004
    • Nudler, E. and Mironov, A. S. (2004) The riboswitch control of bacterial metabolism Trends Biochem. Sci. 29, 11-17 (Pubitemid 38068475)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.1 , pp. 11-17
    • Nudler, E.1    Mironov, A.S.2
  • 6
    • 1642586299 scopus 로고    scopus 로고
    • Control of gene expression by a natural metabolite-responsive ribozyme
    • DOI 10.1038/nature02362
    • Winkler, W. C., Nahvi, A., Roth, A., Collins, J. A., and Breaker, R. R. (2004) Control of gene expression by a natural metabolite-responsive ribozyme Nature 428, 281-286 (Pubitemid 38418792)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 281-286
    • Winkler, W.C.1    Nahvi, A.2    Roth, A.3    Collins, J.A.4    Breaker, R.R.5
  • 8
    • 0037013983 scopus 로고    scopus 로고
    • Glucosamine-6-phosphate synthase: The multi-facets enzyme
    • Milewski, S. (2002) Glucosamine-6-phosphate synthase: The multi-facets enzyme Biochim. Biophys. Acta 1597, 173-192
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 173-192
    • Milewski, S.1
  • 9
    • 37249040135 scopus 로고    scopus 로고
    • Mechanism of mRNA destabilization by the glmS ribozyme
    • DOI 10.1101/gad.1605307
    • Collins, J. A., Irnov, I., Baker, S., and Winkler, W. C. (2007) Mechanism of mRNA destabilization by the glmS ribozyme Genes Dev. 21, 3356-3368 (Pubitemid 350277761)
    • (2007) Genes and Development , vol.21 , Issue.24 , pp. 3356-3368
    • Collins, J.A.1    Irnov, I.2    Baker, S.3    Winkler, W.C.4
  • 11
    • 33947728975 scopus 로고    scopus 로고
    • Trans-acting glmS catalytic riboswitch: Locked and loaded
    • DOI 10.1261/rna.341807
    • Tinsley, R. A., Furchak, J. R., and Walter, N. G. (2007) Trans-acting glmS catalytic riboswitch: Locked and loaded RNA 13, 468-477 (Pubitemid 46506930)
    • (2007) RNA , vol.13 , Issue.4 , pp. 468-477
    • Tinsley, R.A.1    Furchak, J.R.W.2    Walter, N.G.3
  • 12
    • 33846279049 scopus 로고    scopus 로고
    • Structural investigation of the GlmS ribozyme bound to its catalytic cofactor
    • DOI 10.1016/j.chembiol.2006.12.005, PII S1074552106004601
    • Cochrane, J. C., Lipchock, S. V., and Strobel, S. A. (2007) Structural investigation of the GlmS ribozyme bound to its catalytic cofactor Chem. Biol. 14, 97-105 (Pubitemid 46124067)
    • (2007) Chemistry and Biology , vol.14 , Issue.1 , pp. 97-105
    • Cochrane, J.C.1    Lipchock, S.V.2    Strobel, S.A.3
  • 13
    • 33746920364 scopus 로고    scopus 로고
    • Evidence for preorganization of the glmS ribozyme ligand binding pocket
    • DOI 10.1021/bi060337z
    • Hampel, K. J. and Tinsley, M. M. (2006) Evidence for preorganization of the glmS ribozyme ligand binding pocket Biochemistry 45, 7861-7871 (Pubitemid 44185503)
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7861-7871
    • Hampel, K.J.1    Tinsley, M.M.2
  • 14
    • 33748325570 scopus 로고    scopus 로고
    • Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
    • DOI 10.1126/science.1129666
    • Klein, D. J. and Ferré-D'Amaré, A. R. (2006) Structural basis of glmS ribozyme activation by glucosamine-6-phosphate Science 313, 1752-1756 (Pubitemid 44454144)
    • (2006) Science , vol.313 , Issue.5794 , pp. 1752-1756
    • Klein, D.J.1    Ferre-D'Amare, A.R.2
  • 15
    • 65249184394 scopus 로고    scopus 로고
    • Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme
    • Cochrane, J. C., Lipchock, S. V., Smith, K. D., and Strobel, S. A. (2009) Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme Biochemistry 48, 3239-3246
    • (2009) Biochemistry , vol.48 , pp. 3239-3246
    • Cochrane, J.C.1    Lipchock, S.V.2    Smith, K.D.3    Strobel, S.A.4
  • 16
    • 67649207845 scopus 로고    scopus 로고
    • A rate-limiting conformational step in the catalytic pathway of the glmS ribozyme
    • Brooks, K. M. and Hampel, K. J. (2009) A rate-limiting conformational step in the catalytic pathway of the glmS ribozyme Biochemistry 48, 5669-5678
    • (2009) Biochemistry , vol.48 , pp. 5669-5678
    • Brooks, K.M.1    Hampel, K.J.2
  • 17
    • 33645462033 scopus 로고    scopus 로고
    • Characteristics of the glmS ribozyme suggest only structural roles for divalent metal ions
    • Roth, A., Nahvi, A., Lee, M., Jona, I., and Breaker, R. R. (2006) Characteristics of the glmS ribozyme suggest only structural roles for divalent metal ions RNA 12, 607-619
    • (2006) RNA , vol.12 , pp. 607-619
    • Roth, A.1    Nahvi, A.2    Lee, M.3    Jona, I.4    Breaker, R.R.5
  • 18
    • 27744525243 scopus 로고    scopus 로고
    • Ligand requirements for glmS ribozyme self-cleavage
    • DOI 10.1016/j.chembiol.2005.09.006, PII S1074552105002954
    • McCarthy, T. J., Plog, M. A., Floy, S. A., Jansen, J. A., Soukup, J. K., and Soukup, G. A. (2005) Ligand requirements for glmS ribozyme self-cleavage Chem. Biol. 12, 1221-1226 (Pubitemid 41628257)
    • (2005) Chemistry and Biology , vol.12 , Issue.11 , pp. 1221-1226
    • McCarthy, T.J.1    Plog, M.A.2    Floy, S.A.3    Jansen, J.A.4    Soukup, J.K.5    Soukup, G.A.6
  • 19
    • 44149111872 scopus 로고    scopus 로고
    • Riboswitch effectors as protein enzyme cofactors
    • DOI 10.1261/rna.908408
    • Cochrane, J. C. and Strobel, S. A. (2008) Riboswitch effectors as protein enzyme cofactors RNA 14, 993-1002 (Pubitemid 351717480)
    • (2008) RNA , vol.14 , Issue.6 , pp. 993-1002
    • Cochrane, J.C.1    Strobel, S.A.2
  • 20
    • 33744936038 scopus 로고    scopus 로고
    • Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme
    • DOI 10.1038/nsmb1094, PII N1094
    • Jansen, J. A., McCarthy, T. J., Soukup, G. A., and Soukup, J. K. (2006) Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme Nat. Struct. Mol. Biol. 13, 517-523 (Pubitemid 43848906)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 517-523
    • Jansen, J.A.1    McCarthy, T.J.2    Soukup, G.A.3    Soukup, J.K.4
  • 21
    • 34548591567 scopus 로고    scopus 로고
    • Requirement of Helix P2.2 and Nucleotide G1 for Positioning the Cleavage Site and Cofactor of the glmS Ribozyme
    • DOI 10.1016/j.jmb.2007.07.062, PII S0022283607010285
    • Klein, D. J., Wilkinson, S. R., Been, M. D., and Ferre-D'Amare, A. R. (2007) Requirement of helix P2.2 and nucleotide G1 for positioning the cleavage site and cofactor of the glmS ribozyme J. Mol. Biol. 373, 178-189 (Pubitemid 47390720)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.1 , pp. 178-189
    • Klein, D.J.1    Wilkinson, S.R.2    Been, M.D.3    Ferre-D'Amare, A.R.4
  • 22
    • 0038170015 scopus 로고    scopus 로고
    • Metal ion binding to catalytic RNA molecules
    • DeRose, V. J. (2003) Metal ion binding to catalytic RNA molecules Curr. Opin. Struct. Biol. 13, 317-324
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 317-324
    • Derose, V.J.1
  • 23
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • DOI 10.1261/rna.5205404
    • Draper, D. E. (2004) A guide to ions and RNA structure RNA 10, 335-343 (Pubitemid 38240993)
    • (2004) RNA , vol.10 , Issue.3 , pp. 335-343
    • Draper, D.E.1
  • 24
    • 0032192761 scopus 로고    scopus 로고
    • The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone
    • Murray, J. B., Seyhan, A. A., Walter, N. G., Burke, J. M., and Scott, W. G. (1998) The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone Chem. Biol. 5, 587-595 (Pubitemid 29000118)
    • (1998) Chemistry and Biology , vol.5 , Issue.10 , pp. 587-595
    • Murray, J.B.1    Seyhan, A.A.2    Walter, N.G.3    Burke, J.M.4    Scott, W.G.5
  • 25
    • 0031215134 scopus 로고    scopus 로고
    • An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis
    • Nesbitt, S., Hegg, L. A., and Fedor, M. J. (1997) An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis Chem. Biol. 4, 619-630 (Pubitemid 27398764)
    • (1997) Chemistry and Biology , vol.4 , Issue.8 , pp. 619-630
    • Nesbitt, S.1    Hegg, L.A.2    Fedor, M.J.3
  • 26
    • 55249114833 scopus 로고    scopus 로고
    • Structural insights into amino acid binding and gene control by a lysine riboswitch
    • Serganov, A., Huang, L., and Patel, D. J. (2008) Structural insights into amino acid binding and gene control by a lysine riboswitch Nature 455, 1263-1267
    • (2008) Nature , vol.455 , pp. 1263-1267
    • Serganov, A.1    Huang, L.2    Patel, D.J.3
  • 27
    • 52949104434 scopus 로고    scopus 로고
    • Metal ion specificities for folding and cleavage activity in the Schistosoma hammerhead ribozyme
    • Boots, J. L., Canny, M. D., Azimi, E., and Pardi, A. (2008) Metal ion specificities for folding and cleavage activity in the Schistosoma hammerhead ribozyme RNA 14, 2212-2222
    • (2008) RNA , vol.14 , pp. 2212-2222
    • Boots, J.L.1    Canny, M.D.2    Azimi, E.3    Pardi, A.4
  • 28
    • 33847691104 scopus 로고    scopus 로고
    • Structural roles of monovalent cations in the HDV ribozyme
    • DOI 10.1016/j.str.2007.01.017, PII S0969212607000731
    • Ke, A., Ding, F., Batchelor, J. D., and Doudna, J. A. (2007) Structural roles of monovalent cations in the HDV ribozyme Structure 15, 281-287 (Pubitemid 46366724)
    • (2007) Structure , vol.15 , Issue.3 , pp. 281-287
    • Ke, A.1    Ding, F.2    Batchelor, J.D.3    Doudna, J.A.4
  • 29
    • 33745700326 scopus 로고    scopus 로고
    • Cations and hydration in catalytic RNA: Molecular dynamics of the hepatitis delta virus ribozyme
    • Krasovska, M. V., Sefcikova, J., Reblova, K., Schneider, B., Walter, N. G., and Sponer, J. (2006) Cations and hydration in catalytic RNA: Molecular dynamics of the hepatitis delta virus ribozyme Biophys. J. 91, 626-638
    • (2006) Biophys. J. , vol.91 , pp. 626-638
    • Krasovska, M.V.1    Sefcikova, J.2    Reblova, K.3    Schneider, B.4    Walter, N.G.5    Sponer, J.6
  • 30
    • 34447521717 scopus 로고    scopus 로고
    • Low specificity of metal ion binding in the metal ion core of a folded RNA
    • DOI 10.1261/rna.566007
    • Travers, K. J., Boyd, N., and Herschlag, D. (2007) Low specificity of metal ion binding in the metal ion core of a folded RNA RNA 13, 1205-1213 (Pubitemid 47080466)
    • (2007) RNA , vol.13 , Issue.8 , pp. 1205-1213
    • Travers, K.J.1    Boyd, N.2    Herschlag, D.3
  • 31
    • 0034711001 scopus 로고    scopus 로고
    • Kinetic characterization of the second step of group II intron splicing: Role of metal ions and the cleavage site 2′-OH in catalysis
    • Gordon, P. M., Sontheimer, E. J., and Piccirilli, J. A. (2000) Kinetic characterization of the second step of group II intron splicing: role of metal ions and the cleavage site 2′-OH in catalysis Biochemistry 39, 12939-12952
    • (2000) Biochemistry , vol.39 , pp. 12939-12952
    • Gordon, P.M.1    Sontheimer, E.J.2    Piccirilli, J.A.3
  • 33
    • 0033600571 scopus 로고    scopus 로고
    • Probing the role of metal ions in RNA catalysis: Kinetic and thermodynamic characterization of a metal ion interaction with the 2′-moiety of the guanosine nucleophile in the Tetrahymena group i ribozyme
    • Shan, S. O. and Herschlag, D. (1999) Probing the role of metal ions in RNA catalysis: Kinetic and thermodynamic characterization of a metal ion interaction with the 2′-moiety of the guanosine nucleophile in the Tetrahymena group I ribozyme Biochemistry 38, 10958-10975
    • (1999) Biochemistry , vol.38 , pp. 10958-10975
    • Shan, S.O.1    Herschlag, D.2
  • 34
    • 0036894697 scopus 로고    scopus 로고
    • Monovalent cations mediate formation of native tertiary structure of the Tetrahymena thermophila ribozyme
    • DOI 10.1038/nsb871
    • Takamoto, K., He, Q., Morris, S., Chance, M. R., and Brenowitz, M. (2002) Monovalent cations mediate formation of native tertiary structure of the Tetrahymena thermophila ribozyme Nat. Struct. Biol. 9, 928-933 (Pubitemid 35417062)
    • (2002) Nature Structural Biology , vol.9 , Issue.12 , pp. 928-933
    • Takamoto, K.1    He, Q.2    Morris, S.3    Chance, M.R.4    Brenowitz, M.5
  • 35
    • 78650028802 scopus 로고    scopus 로고
    • Analysis of metal ion dependence in glmS ribozyme self-cleavage and coenzyme binding
    • Klawuhn, K., Jansen, J. A., Souchek, J., Soukup, G. A., and Soukup, J. K. (2010) Analysis of metal ion dependence in glmS ribozyme self-cleavage and coenzyme binding ChemBioChem 11, 2567-2571
    • (2010) ChemBioChem , vol.11 , pp. 2567-2571
    • Klawuhn, K.1    Jansen, J.A.2    Souchek, J.3    Soukup, G.A.4    Soukup, J.K.5
  • 36
    • 0034607544 scopus 로고    scopus 로고
    • Probing non-selective cation binding in the hairpin ribozyme with Tb(III)
    • Walter, N. G., Yang, N., and Burke, J. M. (2000) Probing non-selective cation binding in the hairpin ribozyme with Tb(III) J. Mol. Biol. 298, 539-555
    • (2000) J. Mol. Biol. , vol.298 , pp. 539-555
    • Walter, N.G.1    Yang, N.2    Burke, J.M.3
  • 37
    • 0027248444 scopus 로고
    • Novel RNA polymerization reaction catalyzed by a group I ribozyme
    • Chowrira, B. M., Berzal-Herranz, A., and Burke, J. M. (1993) Novel RNA polymerization reaction catalyzed by a group I ribozyme EMBO J. 12, 3599-3605 (Pubitemid 23256446)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3599-3605
    • Chowrira, B.M.1    Berzal-Herranz, A.2    Burke, J.M.3
  • 39
    • 77949905333 scopus 로고    scopus 로고
    • Controlling ribozyme activity by metal ions
    • Schnabl, J. and Sigel, R. K. (2010) Controlling ribozyme activity by metal ions Curr. Opin. Chem. Biol. 14, 269-275
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 269-275
    • Schnabl, J.1    Sigel, R.K.2
  • 40
    • 16244363320 scopus 로고    scopus 로고
    • Metal ions and RNA folding: A highly charged topic with a dynamic future
    • DOI 10.1016/j.cbpa.2005.02.004, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • Woodson, S. A. (2005) Metal ions and RNA folding: A highly charged topic with a dynamic future Curr. Opin. Chem. Biol. 9, 104-109 (Pubitemid 40462481)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 104-109
    • Woodson, S.A.1
  • 43
    • 6344242969 scopus 로고    scopus 로고
    • Principles of RNA compaction: Insights from the equilibrium folding pathway of the P4-P6 RNA domain in monovalent cations
    • DOI 10.1016/j.jmb.2004.08.080, PII S0022283604010800
    • Takamoto, K., Das, R., He, Q., Doniach, S., Brenowitz, M., Herschlag, D., and Chance, M. R. (2004) Principles of RNA compaction: Insights from the equilibrium folding pathway of the P4-P6 RNA domain in monovalent cations J. Mol. Biol. 343, 1195-1206 (Pubitemid 39387820)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1195-1206
    • Takamoto, K.1    Das, R.2    He, Q.3    Doniach, S.4    Brenowitz, M.5    Herschlag, D.6    Chance, M.R.7
  • 44
    • 33749016245 scopus 로고    scopus 로고
    • HDV ribozyme activity in monovalent cations
    • DOI 10.1021/bi061215+
    • Perrotta, A. T. and Been, M. D. (2006) HDV ribozyme activity in monovalent cations Biochemistry 45, 11357-11365 (Pubitemid 44453984)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11357-11365
    • Perrotta, A.T.1    Been, M.D.2
  • 45
    • 0025963132 scopus 로고
    • Visualizing the higher order folding of a catalytic RNA molecule
    • Celander, D. W. and Cech, T. R. (1991) Visualizing the higher order folding of a catalytic RNA molecule Science 251, 401-407 (Pubitemid 21916898)
    • (1991) Science , vol.251 , Issue.4992 , pp. 401-407
    • Gelander, D.W.1    Cech, T.R.2
  • 46
    • 0024976556 scopus 로고
    • Metal ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme
    • Grosshans, C. A. and Cech, T. R. (1989) Metal ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme Biochemistry 28, 6888-6894
    • (1989) Biochemistry , vol.28 , pp. 6888-6894
    • Grosshans, C.A.1    Cech, T.R.2
  • 47
    • 0030750183 scopus 로고    scopus 로고
    • Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction
    • DOI 10.1021/bi9700678
    • McConnell, T. S., Herschlag, D., and Cech, T. R. (1997) Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction Biochemistry 36, 8293-8303 (Pubitemid 27297539)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8293-8303
    • McConnell, T.S.1    Herschlag, D.2    Cech, T.R.3
  • 48
    • 44649098951 scopus 로고    scopus 로고
    • Accommodation of Ca(II) ions for catalytic activity by a group i ribozyme
    • Cernak, P., Madix, R. A., Kuo, L. Y., and Lehman, N. (2008) Accommodation of Ca(II) ions for catalytic activity by a group I ribozyme J. Inorg. Biochem. 102, 1495-1506
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1495-1506
    • Cernak, P.1    Madix, R.A.2    Kuo, L.Y.3    Lehman, N.4
  • 49
    • 34247560640 scopus 로고    scopus 로고
    • A single nucleotide linked to a switch in metal ion reactivity preference in the HDV ribozymes
    • DOI 10.1021/bi602569x
    • Perrotta, A. T. and Been, M. D. (2007) A single nucleotide linked to a switch in metal ion reactivity preference in the HDV ribozymes Biochemistry 46, 5124-5130 (Pubitemid 46683010)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5124-5130
    • Perrotta, A.T.1    Been, M.D.2
  • 51
    • 62249156218 scopus 로고    scopus 로고
    • Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch
    • Serganov, A., Huang, L., and Patel, D. J. (2009) Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch Nature 458, 233-237
    • (2009) Nature , vol.458 , pp. 233-237
    • Serganov, A.1    Huang, L.2    Patel, D.J.3
  • 52
    • 77950292093 scopus 로고    scopus 로고
    • Dissecting electrostatic screening, specific ion binding, and ligand binding in an energetic model for glycine riboswitch folding
    • Lipfert, J., Sim, A. Y., Herschlag, D., and Doniach, S. (2010) Dissecting electrostatic screening, specific ion binding, and ligand binding in an energetic model for glycine riboswitch folding RNA 16, 708-719
    • (2010) RNA , vol.16 , pp. 708-719
    • Lipfert, J.1    Sim, A.Y.2    Herschlag, D.3    Doniach, S.4
  • 53
    • 78649970557 scopus 로고    scopus 로고
    • Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch
    • Huang, L., Serganov, A., and Patel, D. J. (2010) Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch Mol. Cell 40, 774-786
    • (2010) Mol. Cell , vol.40 , pp. 774-786
    • Huang, L.1    Serganov, A.2    Patel, D.J.3
  • 54
    • 77954332068 scopus 로고    scopus 로고
    • Protonation states of the key active site residues and structural dynamics of the glmS riboswitch as revealed by molecular dynamics
    • Banas, P., Walter, N. G., Sponer, J., and Otyepka, M. (2010) Protonation states of the key active site residues and structural dynamics of the glmS riboswitch as revealed by molecular dynamics J. Phys. Chem. B 114, 8701-8712
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8701-8712
    • Banas, P.1    Walter, N.G.2    Sponer, J.3    Otyepka, M.4
  • 55
    • 78649640602 scopus 로고    scopus 로고
    • Deciphering the role of glucosamine-6-phosphate in the riboswitch action of glmS ribozyme
    • Xin, Y. and Hamelberg, D. (2010) Deciphering the role of glucosamine-6-phosphate in the riboswitch action of glmS ribozyme RNA 16, 2455-2463
    • (2010) RNA , vol.16 , pp. 2455-2463
    • Xin, Y.1    Hamelberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.