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Volumn 492, Issue 7427, 2012, Pages 133-137

B12 cofactors directly stabilize an mRNA regulatory switch

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; CYANOCOBALAMIN; LIGAND; MESSENGER RNA; MOLECULAR SCAFFOLD;

EID: 84870539710     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature11607     Document Type: Letter
Times cited : (162)

References (40)
  • 1
    • 84863878432 scopus 로고    scopus 로고
    • Riboswitches:Structuresand mechanisms. Cold Spring Harb. Perspect
    • Garst, A. D., Edwards, A. L.& Batey, R.T. Riboswitches:structuresand mechanisms. Cold Spring Harb. Perspect. Biol. 3, a003533 (2011).
    • (2011) Biol , vol.3
    • Garst, A.D.1    Edwards, A.L.2    Batey, R.T.3
  • 2
    • 84863923278 scopus 로고    scopus 로고
    • Riboswitchesand the RNA world. Cold Spring Harb
    • Breaker, R. R. Riboswitchesand the RNA world. Cold Spring Harb. Perspect Biol. 4, a003566 (2012).
    • (2012) Perspect Biol , vol.4
    • Breaker, R.R.1
  • 3
    • 0026081530 scopus 로고
    • Transcribed sequences of the Escherichia coli btuB gene control its expression and regulation by vitamin B12
    • Lundrigan, M. D., Koster, W. & Kadner, R. J. Transcribed sequences of the Escherichia coli btuB gene control its expression and regulation by vitamin B12. Proc. Natl Acad. Sci. USA 88, 1479-1483 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1479-1483
    • Lundrigan, M.D.1    Koster, W.2    Kadner, R.J.3
  • 4
    • 0030958772 scopus 로고    scopus 로고
    • Multiple transcribed elements control expression of the Escherichia coli btuB gene
    • Franklund, C. V. & Kadner, R.J. Multiple transcribed elements control expression of the Escherichia coli btuB gene. J. Bacteriol. 179, 4039-4042 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 4039-4042
    • Franklund, C.V.1    Kadner, R.J.2
  • 5
    • 1242320304 scopus 로고    scopus 로고
    • Coenzyme B12 riboswitches are widespread genetic control elements in prokaryotes
    • Nahvi, A., Barrick, J. E. & Breaker, R. R. Coenzyme B12 riboswitches are widespread genetic control elements in prokaryotes. Nucleic Acids Res. 32, 143-150 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. 143-150
    • Nahvi, A.1    Barrick, J.E.2    Breaker, R.R.3
  • 6
    • 0036753365 scopus 로고    scopus 로고
    • Genetic control by a metabolite binding mRNA
    • Nahvi, A. etal. Genetic control by a metabolite binding mRNA. Chem. Biol. 9, 1043 (2002).
    • (2002) Chem. Biol , vol.9 , pp. 1043
    • Nahvi, A.1
  • 7
    • 0142071742 scopus 로고    scopus 로고
    • Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes
    • Rodionov, D. A., Vitreschak, A. G., Mironov, A. A. & Gelfand, M. S. Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes. J. Biol. Chem. 278, 41148-41159 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 41148-41159
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 8
    • 0042834096 scopus 로고    scopus 로고
    • Regulation of the vitamin B12 metabolism and transport in bacteria by a conserved RNA structural element
    • Vitreschak, A. G., Rodionov, D. A., Mironov, A. A. & Gelfand, M. S. Regulation of the vitamin B12 metabolism and transport in bacteria by a conserved RNA structural element. RNA 9, 1084-1097 (2003).
    • (2003) RNA , vol.9 , pp. 1084-1097
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 9
    • 46349083026 scopus 로고    scopus 로고
    • The distributions, mechanisms, and structures of metabolite-binding riboswitches
    • Barrick, J. E. & Breaker, R. R. The distributions, mechanisms, and structures of metabolite-binding riboswitches. Genome Biol. 8, R239 (2007).
    • (2007) Genome Biol , vol.8
    • Barrick, J.E.1    Breaker, R.R.2
  • 10
    • 58149191274 scopus 로고    scopus 로고
    • Rfam: Updates to the RNA families database
    • Gardner, P. P. etal. Rfam: updates to the RNA families database. Nucleic Acids Res. 37, D136-D140 (2009).
    • (2009) Nucleic Acids Res , vol.37
    • Gardner, P.P.1
  • 11
    • 63149194170 scopus 로고    scopus 로고
    • Multiple posttranscriptional regulatory mechanisms partner to control ethanolamine utilization in Enterococcus faecalis
    • Fox, K. etal. Multiple posttranscriptional regulatory mechanisms partner to control ethanolamine utilization in Enterococcus faecalis. Proc. Natl Acad. Sci. USA 106, 4435-4440 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4435-4440
    • Fox, K.1
  • 12
    • 33947720028 scopus 로고    scopus 로고
    • Selective 2’-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • Wilkinson, K. A., Merino, E. J. & Weeks, K. M. Selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution. Nature Protocols 1, 1610-1616 (2006).
    • (2006) Nature Protocols , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 13
    • 0024573087 scopus 로고
    • Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB gene regulation
    • Lundrigan, M. D. & Kadner, R. J. Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB gene regulation. J. Bacteriol. 171, 154-161 (1989).
    • (1989) J. Bacteriol , vol.171 , pp. 154-161
    • Lundrigan, M.D.1    Kadner, R.J.2
  • 14
    • 77951606278 scopus 로고    scopus 로고
    • Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes
    • Weinberg, Z. etal. Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes. Genome Biol. 11, R31 (2010).
    • (2010) Genome Biol , vol.11
    • Weinberg, Z.E.1
  • 15
    • 0015838501 scopus 로고
    • Aerobic photolysis of alkylcobalamins: Quantum yields and light-action spectra. Arch. Biochem
    • Taylor, R. T., Smucker, L., Hanna, M. L. & Gill, J. Aerobic photolysis of alkylcobalamins: quantum yields and light-action spectra. Arch. Biochem. Biophys. 156, 521-533 (1973).
    • (1973) Biophys , vol.156 , pp. 521-533
    • Taylor, R.T.1    Smucker, L.2    Hanna, M.L.3    Gill, J.4
  • 16
    • 3042848954 scopus 로고    scopus 로고
    • Crystal structure of a self-splicing group I intron with both exons
    • Adams, P. L., Stahley, M. R., Kosek, A. B., Wang, J.& Strobel, S. A. Crystal structure of a self-splicing group I intron with both exons. Nature 430, 45-50 (2004).
    • (2004) Nature , vol.430 , pp. 45-50
    • Adams, P.L.1    Stahley, M.R.2    Kosek, A.B.3    Wang, J.4    Strobel, S.A.5
  • 17
    • 58549119994 scopus 로고    scopus 로고
    • The UA_handle: A versatile submotif in stable RNA architectures
    • Jaeger, L., Verzemnieks, E. J. & Geary, C. The UA_handle: a versatile submotif in stable RNA architectures. Nucleic Acids Res. 37, 215-230 (2009).
    • (2009) Nucleic Acids Res , vol.37 , pp. 215-230
    • Jaeger, L.1    Verzemnieks, E.J.2    Geary, C.3
  • 18
    • 0036717041 scopus 로고    scopus 로고
    • Frequent occurrence of the T-loop RNA folding motif in ribosomal RNAs
    • Nagaswamy, U. & Fox, G. E. Frequent occurrence of the T-loop RNA folding motif in ribosomal RNAs. RNA 8, 1112-1119(2002).
    • (2002) RNA , vol.8 , pp. 1112-1119
    • Nagaswamy, U.1    Fox, G.E.2
  • 19
    • 0038475947 scopus 로고    scopus 로고
    • On the occurrence of the T-loop RNA folding motif in large RNA molecules
    • Krasilnikov, A. S. & Mondragon, A. On the occurrence of the T-loop RNA folding motif in large RNA molecules. RNA 9, 640-643 (2003).
    • (2003) RNA , vol.9 , pp. 640-643
    • Krasilnikov, A.S.1    Mondragon, A.2
  • 20
    • 62249156218 scopus 로고    scopus 로고
    • Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch
    • Serganov, A., Huang, L. & Patel, D.J. Coenzyme recognition and gene regulation by a flavin mononucleotide riboswitch. Nature 458, 233-237 (2009).
    • (2009) Nature , vol.458 , pp. 233-237
    • Serganov, A.1    Huang, L.2    Patel, D.J.3
  • 21
    • 0033988166 scopus 로고    scopus 로고
    • The structural basisformolecularrecognition by the vitamin B12 RNA aptamer
    • Sussman, D., Nix, J.C. & Wilson, C. The structural basisformolecularrecognition by the vitamin B12 RNA aptamer. Nature Struct Biol. 7, 53-57 (2000).
    • (2000) Nature Struct Biol , vol.7 , pp. 53-57
    • Sussman, D.1    Nix, J.C.2    Wilson, C.3
  • 22
    • 79956323244 scopus 로고    scopus 로고
    • Light-dependent gene regulation by a coenzyme B12-based photoreceptor
    • Ortiz-Guerrero, J. M., Polanco, M. C., Murillo, F. J., Padmanabhan, S. & Elias-Arnanz, M. Light-dependent gene regulation by a coenzyme B12-based photoreceptor. Proc. Natl Acad Sci. USA 108, 7565-7570 (2011).
    • (2011) , vol.108 , pp. 7565-7570
    • Ortiz-Guerrero, J.M.1    Polanco, M.C.2    Murillo, F.J.3    Padmanabhan, S.4    Elias-Arnanz, M.5
  • 23
    • 30944458838 scopus 로고    scopus 로고
    • Atomic level architecture of group I introns revealed
    • Vicens, Q. & Cech, T. R. Atomic level architecture of group I introns revealed. Trends Biochem. Sci. 31, 41-51 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 41-51
    • Vicens, Q.1    Cech, T.R.2
  • 24
    • 84861908221 scopus 로고    scopus 로고
    • One core, two shells: Bacterial and eukaryotic ribosomes
    • Melnikov, S. etal. One core, two shells: bacterial and eukaryotic ribosomes. Nature Struct Mol. Biol. 19, 560-567 (2012).
    • (2012) Nature Struct Mol. Biol. , vol.19 , pp. 560-567
    • Melnikov, S.1
  • 25
    • 57049151833 scopus 로고    scopus 로고
    • Annotation of tertiary interactions in RNA structures reveals variations and correlations
    • Xin, Y., Laing, C., Leontis, N. B. & Schlick, T. Annotation of tertiary interactions in RNA structures reveals variations and correlations. RNA 14, 2465-2477 (2008).
    • (2008) RNA , vol.14 , pp. 2465-2477
    • Xin, Y.1    Laing, C.2    Leontis, N.B.3    Schlick, T.4
  • 26
    • 84255189090 scopus 로고    scopus 로고
    • The molecular interactions that stabilize RNA tertiary structure: RNA motifs, patterns, and networks
    • Butcher, S. E. & Pyle, A. M. The molecular interactions that stabilize RNA tertiary structure: RNA motifs, patterns, and networks. Acc. Chem. Res. 44, 1302-1311 (2011).
    • (2011) Acc. Chem. Res , vol.44 , pp. 1302-1311
    • Butcher, S.E.1    Pyle, A.M.2
  • 27
    • 0029058784 scopus 로고
    • Determinants of RNA hairpin loop-loop complex stability
    • Gregorian, R. S. Jr & Crothers, D. M. Determinants of RNA hairpin loop-loop complex stability. J. Mol. Biol. 248, 968-984 (1995).
    • (1995) J. Mol. Biol , vol.248 , pp. 968-984
    • Gregorian, R.S.1    Crothers, D.M.2
  • 28
    • 0036940303 scopus 로고    scopus 로고
    • A. M. Metal ions in the structure and function of RNA
    • I. Pyle, A. M. Metal ions in the structure and function of RNA. J. Biol. Inorg. Chem. 7, 679-690 (2002).
    • (2002) J. Biol. Inorg. Chem , vol.7 , pp. 679-690
    • Pyle, I.1
  • 29
  • 30
    • 69449089715 scopus 로고    scopus 로고
    • Determining structures of RNAaptamers and riboswitches by X-ray crystallography
    • Edwards, A. L., Garst, A. D. & Batey, R. T. Determining structures of RNAaptamers and riboswitches by X-ray crystallography. Methods Mol. Biol. 535, 135-163 (2009).
    • (2009) Methods Mol. Biol , vol.535 , pp. 135-163
    • Edwards, A.L.1    Garst, A.D.2    Batey, R.T.3
  • 31
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan, J. F. & Uhlenbeck, O. C. Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol. 180, 51-62 (1989).
    • (1989) Methods Enzymol , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 32
    • 65649133549 scopus 로고    scopus 로고
    • Monitoring RNA-ligand interactions using isothermal titration calorimetry
    • Gilbert, S. D. & Batey, R. T. Monitoring RNA-ligand interactions using isothermal titration calorimetry. Methods Mol. Biol. 540, 97-114(2009).
    • (2009) Methods Mol. Biol. , vol.540 , pp. 97-114
    • Gilbert, S.D.1    Batey, R.T.2
  • 33
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol
    • Baba, T. etal. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst Biol. 2, 2006-2008 (2006).
    • (2006) Syst Biol , vol.2 , pp. 2006-2008
    • Baba, T.1
  • 34
    • 79953733151 scopus 로고    scopus 로고
    • Data processing and analysis with the autoPROc toolbox
    • Vonrhein, C. etal. Data processing and analysis with the autoPROc toolbox. Acta Crystallogr. D 67, 293-302 (2011).
    • (2011) Acta Crystallogr. , vol.D67 , pp. 293-302
    • Vonrhein, C.1
  • 35
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. etal. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. , vol.D58 , pp. 1948-1954
    • Adams, P.D.1
  • 37
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • Blanc, E. etal. Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT. Acta Crystallogr. D 60, 2210-2221 (2004).
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2210-2221
    • Blanc, E.1
  • 38
    • 77952352777 scopus 로고    scopus 로고
    • Semiautomated model building for RNAcrystallography using a directed rotameric approach
    • Keating, K. S. & Pyle, A. M. Semiautomated model building for RNAcrystallography using a directed rotameric approach. Proc. Natl Acad. Sci. USA 107, 8177-8182 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8177-8182
    • Keating, K.S.1    Pyle, A.M.2
  • 39
    • 77957111493 scopus 로고    scopus 로고
    • Use of the spliceosomal protein U1A to facilitate crystallization and structure determination of complex RNAs
    • Ferré-D'Amaré, A. R. Use of the spliceosomal protein U1A to facilitate crystallization and structure determination of complex RNAs. Methods 52, 159-167 (2010).
    • (2010) Methods , vol.52 , pp. 159-167
    • Ferré-D'amaré, A.R.1
  • 40
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. etal. Phaser crystallographic software. J.Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • Mc Coy, A.J.1


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