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Volumn 17, Issue 1, 2011, Pages 74-84

Identification of a tertiary interaction important for cooperative ligand binding by the glycine riboswitch

Author keywords

Aptamers; Cooperativity; Glycine; Riboswit

Indexed keywords

APTAMER; GLYCINE;

EID: 78650424317     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2271511     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 84935023004 scopus 로고
    • Uber einen in biologischen beziehung wichtigen einfluss, den die kohlen-suer-spannung des blutes auf dessen sauerstoffbindung ubt
    • Bohr C, Hasselbach KA, Krogh A. 1904. Uber einen in biologischen beziehung wichtigen einfluss, den die kohlen-suer-spannung des blutes auf dessen sauerstoffbindung ubt. Skand Arch Physiol 15: 401-412.
    • (1904) Skand Arch Physiol , vol.15 , pp. 401-412
    • Bohr, C.1    Hasselbach, K.A.2    Krogh, A.3
  • 2
    • 0032623279 scopus 로고    scopus 로고
    • PACE analysis of RNA-peptide interactions
    • Cilley CD, Williamson JR. 1999. PACE analysis of RNA-peptide interactions. Methods Mol Biol 118: 129-141.
    • (1999) Methods Mol Biol , vol.118 , pp. 129-141
    • Cilley, C.D.1    Williamson, J.R.2
  • 5
    • 0028804927 scopus 로고
    • Cooperativity: Over the Hill
    • Forsen S, Linse S. 1995. Cooperativity: Over the Hill. Trends Biochem Sci 20: 495-497.
    • (1995) Trends Biochem Sci , vol.20 , pp. 495-497
    • Forsen, S.1    Linse, S.2
  • 6
    • 33644792751 scopus 로고    scopus 로고
    • The S(MK) box is a new SAM-binding RNA for translational regulation of SAM synthetase
    • Fuchs RT, Grundy FJ, Henkin TM. 2006. The S(MK) box is a new SAM-binding RNA for translational regulation of SAM synthetase. Nat Struct Mol Biol 13: 226-233.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 226-233
    • Fuchs, R.T.1    Grundy, F.J.2    Henkin, T.M.3
  • 7
    • 0036071391 scopus 로고    scopus 로고
    • GU receptors of double helices mediate tRNA movement in the ribosome
    • Gagnon MG, Steinberg SV. 2002. GU receptors of double helices mediate tRNA movement in the ribosome. RNA 8: 873-877.
    • (2002) RNA , vol.8 , pp. 873-877
    • Gagnon, M.G.1    Steinberg, S.V.2
  • 8
    • 33846026769 scopus 로고    scopus 로고
    • Close packing of helices 3 and 12 of 16S rRNA is required for normal ribosome function
    • Gagnon MG, Mukhopadhyay A, Steinberg SV. 2006. Close packing of helices 3 and 12 of 16S rRNA is required for normal ribosome function. J Biol Chem 281: 39349-39357.
    • (2006) J Biol Chem , vol.281 , pp. 39349-39357
    • Gagnon, M.G.1    Mukhopadhyay, A.2    Steinberg, S.V.3
  • 10
    • 0142123125 scopus 로고    scopus 로고
    • The L box regulon: Lysine sensing by leader RNAs of bacterial lysine biosynthesis genes
    • Grundy FJ, Lehman SC, Henkin TM. 2003. The L box regulon: Lysine sensing by leader RNAs of bacterial lysine biosynthesis genes. Proc Natl Acad Sci 100: 12057-12062.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 12057-12062
    • Grundy, F.J.1    Lehman, S.C.2    Henkin, T.M.3
  • 11
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill AV. 1910. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J Physiol 40: iv-vii.
    • (1910) J Physiol , vol.40
    • Hill, A.V.1
  • 12
    • 0035312243 scopus 로고    scopus 로고
    • Cooperative binding of effectors by an allosteric ribozyme
    • Jose AM, Soukup GA, Breaker RR. 2001. Cooperative binding of effectors by an allosteric ribozyme. Nucleic Acids Res 29: 1631-1637.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1631-1637
    • Jose, A.M.1    Soukup, G.A.2    Breaker, R.R.3
  • 13
    • 0032755647 scopus 로고    scopus 로고
    • Allosteric selection of ribozymes that respond to the second messengers cGMP and cAMP
    • Koizumi M, Soukup GA, Kerr JN, Breaker RR. 1999. Allosteric selection of ribozymes that respond to the second messengers cGMP and cAMP. Nat Struct Biol 6: 1062-1071.
    • (1999) Nat Struct Biol , vol.6 , pp. 1062-1071
    • Koizumi, M.1    Soukup, G.A.2    Kerr, J.N.3    Breaker, R.R.4
  • 14
    • 0037033008 scopus 로고    scopus 로고
    • Proteomics and models for enzyme cooperativity
    • Koshland DE Jr, Hamadani K. 2002. Proteomics and models for enzyme cooperativity. J Biol Chem 277: 46841-46844.
    • (2002) J Biol Chem , vol.277 , pp. 46841-46844
    • Koshland Jr., D.E.1    Hamadani, K.2
  • 15
    • 38049025288 scopus 로고    scopus 로고
    • Chemical basis of glycine riboswitch cooperativity
    • Kwon M, Strobel SA. 2008. Chemical basis of glycine riboswitch cooperativity. RNA 14: 25-34.
    • (2008) RNA , vol.14 , pp. 25-34
    • Kwon, M.1    Strobel, S.A.2
  • 16
    • 70349238567 scopus 로고    scopus 로고
    • Tertiary motifs revealed in analyses of higher-order RNA junctions
    • Laing C, Jung S, Iqbal A, Schlick T. 2009. Tertiary motifs revealed in analyses of higher-order RNA junctions. J Mol Biol 393: 67-82.
    • (2009) J Mol Biol , vol.393 , pp. 67-82
    • Laing, C.1    Jung, S.2    Iqbal, A.3    Schlick, T.4
  • 17
    • 33845971464 scopus 로고    scopus 로고
    • Structural transitions and thermodynamics of a glycine-dependent riboswitch from Vibrio cholerae
    • Lipfert J, Das R, Chu VB, Kudaravalli M, Boyd N, Herschlag D, Doniach S. 2007. Structural transitions and thermodynamics of a glycine-dependent riboswitch from Vibrio cholerae. J Mol Biol 365: 1393-1406.
    • (2007) J Mol Biol , vol.365 , pp. 1393-1406
    • Lipfert, J.1    Das, R.2    Chu, V.B.3    Kudaravalli, M.4    Boyd, N.5    Herschlag, D.6    Doniach, S.7
  • 19
    • 0038210214 scopus 로고    scopus 로고
    • Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria
    • Mandal M, Boese B, Barrick JE, Winkler WC, Breaker RR. 2003. Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria. Cell 113: 577-586.
    • (2003) Cell , vol.113 , pp. 577-586
    • Mandal, M.1    Boese, B.2    Barrick, J.E.3    Winkler, W.C.4    Breaker, R.R.5
  • 21
    • 33745628336 scopus 로고    scopus 로고
    • Structure of the S-adenosylmethionine riboswitch regulatory mRNA element
    • Montange RK, Batey RT. 2006. Structure of the S-adenosylmethionine riboswitch regulatory mRNA element. Nature 441: 1172-1175.
    • (2006) Nature , vol.441 , pp. 1172-1175
    • Montange, R.K.1    Batey, R.T.2
  • 22
    • 0032530539 scopus 로고    scopus 로고
    • Identifying RNA minor groove tertiary contacts by nucleotide analogue interference mapping with N2-methylguanosine
    • Ortoleva-Donnelly L, Kronman M, Strobel SA. 1998. Identifying RNA minor groove tertiary contacts by nucleotide analogue interference mapping with N2-methylguanosine. Biochemistry 37: 12933-12942.
    • (1998) Biochemistry , vol.37 , pp. 12933-12942
    • Ortoleva-Donnelly, L.1    Kronman, M.2    Strobel, S.A.3
  • 23
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz MF. 1989. Mechanisms of cooperativity and allosteric regulation in proteins. Q Rev Biophys 22: 139-237.
    • (1989) Q Rev Biophys , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 24
    • 0028857011 scopus 로고
    • What species is responsible for strand scission in the reaction of [Fe(EDTA)] 2-and H2O2 with DNA?
    • Pogozelski WK, McNeese TJ, Tullius TD. 1995. What species is responsible for strand scission in the reaction of [Fe(EDTA)]2-and H2O2 with DNA? J Am Chem Soc 117: 6428-6433.
    • (1995) J Am Chem Soc , vol.117 , pp. 6428-6433
    • Pogozelski, W.K.1    McNeese, T.J.2    Tullius, T.D.3
  • 25
    • 84897585709 scopus 로고    scopus 로고
    • In-line probing analysis of riboswitches
    • Regulski EE, Breaker RR. 2008. In-line probing analysis of riboswitches. Methods Mol Biol 419: 53-67.
    • (2008) Methods Mol Biol , vol.419 , pp. 53-67
    • Regulski, E.E.1    Breaker, R.R.2
  • 26
    • 0032529298 scopus 로고    scopus 로고
    • N 2-methylguanosine is iso-energetic with guanosine in RNA duplexes and GNRA tetraloops
    • Rife JP, Cheng CS, Moore PB, Strobel SA. 1998. N 2-methylguanosine is iso-energetic with guanosine in RNA duplexes and GNRA tetraloops. Nucleic Acids Res 26: 3640-3644.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3640-3644
    • Rife, J.P.1    Cheng, C.S.2    Moore, P.B.3    Strobel, S.A.4
  • 27
    • 67650713931 scopus 로고    scopus 로고
    • The structural and functional diversity of metabolite-binding riboswitches
    • Roth A, Breaker RR. 2009. The structural and functional diversity of metabolite-binding riboswitches. Annu Rev Biochem 78: 305-334.
    • (2009) Annu Rev Biochem , vol.78 , pp. 305-334
    • Roth, A.1    Breaker, R.R.2
  • 28
    • 0035336687 scopus 로고    scopus 로고
    • Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms
    • Royer WE Jr, Knapp JE, Strand K, Heaslet HA. 2001. Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms. Trends Biochem Sci 26: 297-304.
    • (2001) Trends Biochem Sci , vol.26 , pp. 297-304
    • Royer Jr., W.E.1    Knapp, J.E.2    Strand, K.3    Heaslet, H.A.4
  • 29
    • 0032860382 scopus 로고    scopus 로고
    • Nucleotide analog interference mapping
    • Ryder SP, Strobel SA. 1999. Nucleotide analog interference mapping. Methods 18: 38-50.
    • (1999) Methods , vol.18 , pp. 38-50
    • Ryder, S.P.1    Strobel, S.A.2
  • 30
    • 71849091911 scopus 로고    scopus 로고
    • Amino acid recognition and gene regulation by riboswitches
    • Serganov A, Patel DJ. 2009. Amino acid recognition and gene regulation by riboswitches. Biochim Biophys Acta 1789: 592-611.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 592-611
    • Serganov, A.1    Patel, D.J.2
  • 31
    • 55249114833 scopus 로고    scopus 로고
    • Structure insights into aminoacid binding and gene control by a lysine riboswitch
    • Serganov A, Huang L, Patel DJ. 2008. Structure insights into aminoacid 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
  • 33
    • 0242298623 scopus 로고    scopus 로고
    • An mRNA structure in bacteria that controls gene expression by binding lysine
    • DOI 10.1101/gad.1140003
    • Sudarsan N, Wickiser JK, Nakamura S, Ebert MS, Breaker RR. 2003. An mRNA structure in bacteria that controls gene expression by binding lysine. Genes Dev 17: 2688-2697. (Pubitemid 37363073)
    • (2003) Genes and Development , vol.17 , Issue.21 , pp. 2688-2697
    • Sudarsan, N.1    Wickiser, J.K.2    Nakamura, S.3    Ebert, M.S.4    Breaker, R.R.5
  • 37
    • 16244389281 scopus 로고    scopus 로고
    • Mapping nucleic acid structure by hydroxyl radical cleavage
    • Tullius TD, Greenbaum JA. 2005. Mapping nucleic acid structure by hydroxyl radical cleavage. Curr Opin Chem Biol 9: 127-134.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 127-134
    • Tullius, T.D.1    Greenbaum, J.A.2
  • 39
    • 33947714417 scopus 로고    scopus 로고
    • Ligand binding and gene control characteristics of tandem riboswitches in Bacillus anthracis
    • Welz R, Breaker RR. 2007. Ligand binding and gene control characteristics of tandem riboswitches in Bacillus anthracis. RNA 13: 573-582.
    • (2007) RNA , vol.13 , pp. 573-582
    • Welz, R.1    Breaker, R.R.2
  • 40
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • Whitty A. 2008. Cooperativity and biological complexity. Nat Chem Biol 4: 435-439.
    • (2008) Nat Chem Biol , vol.4 , pp. 435-439
    • Whitty, A.1
  • 41
    • 27144527479 scopus 로고    scopus 로고
    • Regulation of bacterial gene expression by riboswitches
    • Winkler WC, Breaker RR. 2005. Regulation of bacterial gene expression by riboswitches. Annu Rev Microbiol 59: 487-517.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 487-517
    • Winkler, W.C.1    Breaker, R.R.2
  • 42
    • 0037058920 scopus 로고    scopus 로고
    • An mRNA structure that controls gene expression by binding FMN
    • Winkler WC, Cohen-Chalamish S, Breaker RR. 2002. An mRNA structure that controls gene expression by binding FMN. Proc Natl Acad Sci 99: 15908-15913.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 15908-15913
    • Winkler, W.C.1    Cohen-Chalamish, S.2    Breaker, R.R.3
  • 43
    • 0042320361 scopus 로고    scopus 로고
    • An mRNA structure that controls gene expression by binding S-adenosylmethionine
    • DOI 10.1038/nsb967
    • Winkler WC, Nahvi A, Sudarsan N, Barrick JE, Breaker RR. 2003. An mRNA structure that controls gene expression by binding S-adenosylmethionine. Nat Struct Biol 10: 701-707. (Pubitemid 37052407)
    • (2003) Nature Structural Biology , vol.10 , Issue.9 , pp. 701-707
    • Winkler, W.C.1    Nahvi, A.2    Sudarsan, N.3    Barrick, J.E.4    Breaker, R.R.5
  • 44
    • 0033597435 scopus 로고    scopus 로고
    • Mechanism of intrinsic transcription termination and antitermination
    • Yarnell WS, Roberts JW. 1999. Mechanism of intrinsic transcription termination and antitermination. Science 284: 611-615.
    • (1999) Science , vol.284 , pp. 611-615
    • Yarnell, W.S.1    Roberts, J.W.2


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