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Volumn 1839, Issue 10, 2014, Pages 939-950

Structure and function of preQ1 riboswitches

Author keywords

NMR; PreQ0; Queuine; Queuosine; TRNA modification; X ray crystallography

Indexed keywords

ASPARAGINE TRANSFER RNA; ASPARTIC ACID TRANSFER RNA; HISTIDINE TRANSFER RNA; QUEUOSINE; TYROSINE TRANSFER RNA;

EID: 84908067356     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.04.019     Document Type: Review
Times cited : (35)

References (87)
  • 1
    • 38849103659 scopus 로고    scopus 로고
    • Purine sensing by riboswitches
    • Kim J.N., Breaker R.R. Purine sensing by riboswitches. Biol. Cell 2008, 100:1-11.
    • (2008) Biol. Cell , vol.100 , pp. 1-11
    • Kim, J.N.1    Breaker, R.R.2
  • 2
    • 84865231710 scopus 로고    scopus 로고
    • Structure and mechanism of purine-binding riboswitches
    • Batey R.T. Structure and mechanism of purine-binding riboswitches. Q. Rev. Biophys. 2012, 45:345-381.
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 345-381
    • Batey, R.T.1
  • 4
    • 0015514384 scopus 로고
    • Possible anticodon sequences of tRNA His, tRNA Asm, and tRNA Asp from Escherichia coli B. Universal presence of nucleoside Q in the first position of the anticodons of these transfer ribonucleic acids
    • Harada F., Nishimura S. Possible anticodon sequences of tRNA His, tRNA Asm, and tRNA Asp from Escherichia coli B. Universal presence of nucleoside Q in the first position of the anticodons of these transfer ribonucleic acids. Biochemistry 1972, 11:301-308.
    • (1972) Biochemistry , vol.11 , pp. 301-308
    • Harada, F.1    Nishimura, S.2
  • 5
    • 0034788470 scopus 로고    scopus 로고
    • Queuosine modification of tRNA: a case for convergent evolution
    • Morris R.C., Elliott M.S. Queuosine modification of tRNA: a case for convergent evolution. Mol. Genet. Metab. 2001, 74:147-159.
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 147-159
    • Morris, R.C.1    Elliott, M.S.2
  • 6
    • 43049099252 scopus 로고    scopus 로고
    • An embarrassment of riches: the enzymology of RNA modification
    • Iwata-Reuyl D. An embarrassment of riches: the enzymology of RNA modification. Curr. Opin. Chem. Biol. 2008, 12:126-133.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 126-133
    • Iwata-Reuyl, D.1
  • 7
    • 18844429219 scopus 로고    scopus 로고
    • Transglycosylation: a mechanism for RNA modification (and editing?)
    • Garcia G.A., Kittendorf J.D. Transglycosylation: a mechanism for RNA modification (and editing?). Bioorg. Chem. 2005, 33:229-251.
    • (2005) Bioorg. Chem. , vol.33 , pp. 229-251
    • Garcia, G.A.1    Kittendorf, J.D.2
  • 9
    • 84871436566 scopus 로고    scopus 로고
    • Transfer RNA modifications: nature's combinatorial chemistry playground, Wiley interdisciplinary reviews
    • Jackman J.E., Alfonzo J.D. Transfer RNA modifications: nature's combinatorial chemistry playground, Wiley interdisciplinary reviews. RNA 2013, 4:35-48.
    • (2013) RNA , vol.4 , pp. 35-48
    • Jackman, J.E.1    Alfonzo, J.D.2
  • 10
    • 20144367825 scopus 로고    scopus 로고
    • Structural effects of hypermodified nucleosides in the Escherichia coli and human tRNALys anticodon loop: the effect of nucleosides s2U, mcm5U, mcm5s2U, mnm5s2U, t6A, and ms2t6A
    • Durant P.C., Bajji A.C., Sundaram M., Kumar R.K., Davis D.R. Structural effects of hypermodified nucleosides in the Escherichia coli and human tRNALys anticodon loop: the effect of nucleosides s2U, mcm5U, mcm5s2U, mnm5s2U, t6A, and ms2t6A. Biochemistry 2005, 44:8078-8089.
    • (2005) Biochemistry , vol.44 , pp. 8078-8089
    • Durant, P.C.1    Bajji, A.C.2    Sundaram, M.3    Kumar, R.K.4    Davis, D.R.5
  • 12
    • 80053194776 scopus 로고    scopus 로고
    • Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases
    • Lamichhane T.N., Blewett N.H., Maraia R.J. Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases. RNA 2011, 17:1846-1857.
    • (2011) RNA , vol.17 , pp. 1846-1857
    • Lamichhane, T.N.1    Blewett, N.H.2    Maraia, R.J.3
  • 13
    • 33846269602 scopus 로고    scopus 로고
    • TRNA's wobble decoding of the genome: 40years of modification
    • Agris P.F., Vendeix F.A., Graham W.D. tRNA's wobble decoding of the genome: 40years of modification. J. Mol. Biol. 2007, 366:1-13.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1-13
    • Agris, P.F.1    Vendeix, F.A.2    Graham, W.D.3
  • 15
    • 0025370590 scopus 로고
    • The deazaguanine-derivative, queuine, affects cell proliferation, protein phosphorylation and the expression of the proto oncogenes c-fos and c-myc in HeLa cells
    • Langgut W., Kersten H. The deazaguanine-derivative, queuine, affects cell proliferation, protein phosphorylation and the expression of the proto oncogenes c-fos and c-myc in HeLa cells. FEBS Lett. 1990, 265:33-36.
    • (1990) FEBS Lett. , vol.265 , pp. 33-36
    • Langgut, W.1    Kersten, H.2
  • 16
    • 0027379152 scopus 로고
    • Modulation of mammalian cell proliferation by a modified tRNA base of bacterial origin
    • Langgut W., Reisser T., Nishimura S., Kersten H. Modulation of mammalian cell proliferation by a modified tRNA base of bacterial origin. FEBS Lett. 1993, 336:137-142.
    • (1993) FEBS Lett. , vol.336 , pp. 137-142
    • Langgut, W.1    Reisser, T.2    Nishimura, S.3    Kersten, H.4
  • 17
    • 0025977143 scopus 로고
    • Queuine, a transfer-RNA anticodon wobble base, maintains the proliferative and pluripotent potential of Hl-60 cells in the presence of the differentiating agent 6-thioguanine
    • French B.T., Patrick D.E., Grever M.R., Trewyn R.W. Queuine, a transfer-RNA anticodon wobble base, maintains the proliferative and pluripotent potential of Hl-60 cells in the presence of the differentiating agent 6-thioguanine. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:370-374.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 370-374
    • French, B.T.1    Patrick, D.E.2    Grever, M.R.3    Trewyn, R.W.4
  • 19
    • 0018582874 scopus 로고
    • Alteration of the Q family of transfer RNAs in adult Drosophila melanogaster as a function of age, nutrition, and genotype
    • Owenby R.K., Stulberg M.P., Jacobson K.B. Alteration of the Q family of transfer RNAs in adult Drosophila melanogaster as a function of age, nutrition, and genotype. Mech. Ageing Dev. 1979, 11:91-103.
    • (1979) Mech. Ageing Dev. , vol.11 , pp. 91-103
    • Owenby, R.K.1    Stulberg, M.P.2    Jacobson, K.B.3
  • 20
    • 36549029244 scopus 로고    scopus 로고
    • Possible involvement of queuine in regulation of cell proliferation
    • Pathak C., Jaiswal Y.K., Vinayak M. Possible involvement of queuine in regulation of cell proliferation. BioFactors 2007, 29:159-173.
    • (2007) BioFactors , vol.29 , pp. 159-173
    • Pathak, C.1    Jaiswal, Y.K.2    Vinayak, M.3
  • 21
    • 0015924554 scopus 로고
    • Activity of a transfer RNA modifying enzyme during the development of Drosophila and its relationship to the su(s) locus
    • White B.N., Tener G.M. Activity of a transfer RNA modifying enzyme during the development of Drosophila and its relationship to the su(s) locus. J. Mol. Biol. 1973, 74:635-651.
    • (1973) J. Mol. Biol. , vol.74 , pp. 635-651
    • White, B.N.1    Tener, G.M.2
  • 22
    • 0028353466 scopus 로고
    • The nutrient factor queuine protects HeLa cells from hypoxic stress and improves metabolic adaptation to oxygen availability
    • Reisser T., Langgut W., Kersten H. The nutrient factor queuine protects HeLa cells from hypoxic stress and improves metabolic adaptation to oxygen availability. Eur. J. Biochem./FEBS 1994, 221:979-986.
    • (1994) Eur. J. Biochem./FEBS , vol.221 , pp. 979-986
    • Reisser, T.1    Langgut, W.2    Kersten, H.3
  • 23
    • 0028068635 scopus 로고
    • Deficiency of queuine, a highly modified purine base, in transfer RNAs from primary and metastatic ovarian malignant tumors in women
    • Baranowski W., Dirheimer G., Jakowicki J.A., Keith G. Deficiency of queuine, a highly modified purine base, in transfer RNAs from primary and metastatic ovarian malignant tumors in women. Cancer Res. 1994, 54:4468-4471.
    • (1994) Cancer Res. , vol.54 , pp. 4468-4471
    • Baranowski, W.1    Dirheimer, G.2    Jakowicki, J.A.3    Keith, G.4
  • 24
    • 0022408375 scopus 로고
    • Relationship of queuine-lacking transfer RNA to the grade of malignancy in human leukemias and lymphomas
    • Emmerich B., Zubrod E., Weber H., Maubach P.A., Kersten H., Kersten W. Relationship of queuine-lacking transfer RNA to the grade of malignancy in human leukemias and lymphomas. Cancer Res. 1985, 45:4308-4314.
    • (1985) Cancer Res. , vol.45 , pp. 4308-4314
    • Emmerich, B.1    Zubrod, E.2    Weber, H.3    Maubach, P.A.4    Kersten, H.5    Kersten, W.6
  • 25
    • 0026737277 scopus 로고
    • Relationship of the queuine content of transfer ribonucleic acids to histopathological grading and survival in human lung cancer
    • Huang B.S., Wu R.T., Chien K.Y. Relationship of the queuine content of transfer ribonucleic acids to histopathological grading and survival in human lung cancer. Cancer Res. 1992, 52:4696-4700.
    • (1992) Cancer Res. , vol.52 , pp. 4696-4700
    • Huang, B.S.1    Wu, R.T.2    Chien, K.Y.3
  • 26
    • 0035130319 scopus 로고    scopus 로고
    • Increased expression of queuosine synthesizing enzyme, tRNA-guanine transglycosylase, and queuosine levels in tRNA of leukemic cells
    • Ishiwata S., Katayama J., Shindo H., Ozawa Y., Itoh K., Mizugaki M. Increased expression of queuosine synthesizing enzyme, tRNA-guanine transglycosylase, and queuosine levels in tRNA of leukemic cells. J. Biochem. 2001, 129:13-17.
    • (2001) J. Biochem. , vol.129 , pp. 13-17
    • Ishiwata, S.1    Katayama, J.2    Shindo, H.3    Ozawa, Y.4    Itoh, K.5    Mizugaki, M.6
  • 28
    • 0031566184 scopus 로고    scopus 로고
    • Effects of a diet deficient in tyrosine and queuine on germfree mice
    • Marks T., Farkas W.R. Effects of a diet deficient in tyrosine and queuine on germfree mice. Biochem. Biophys. Res. Commun. 1997, 230:233-237.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 233-237
    • Marks, T.1    Farkas, W.R.2
  • 30
    • 0033965439 scopus 로고    scopus 로고
    • Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: the expression of the virF gene
    • Durand J.M., Dagberg B., Uhlin B.E., Bjork G.R. Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: the expression of the virF gene. Mol. Microbiol. 2000, 35:924-935.
    • (2000) Mol. Microbiol. , vol.35 , pp. 924-935
    • Durand, J.M.1    Dagberg, B.2    Uhlin, B.E.3    Bjork, G.R.4
  • 31
    • 0028041249 scopus 로고
    • VacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of Escherichia coli K-12
    • Durand J.M., Okada N., Tobe T., Watarai M., Fukuda I., Suzuki T., Nakata N., Komatsu K., Yoshikawa M., Sasakawa C. vacC, a virulence-associated chromosomal locus of Shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of Escherichia coli K-12. J. Bacteriol. 1994, 176:4627-4634.
    • (1994) J. Bacteriol. , vol.176 , pp. 4627-4634
    • Durand, J.M.1    Okada, N.2    Tobe, T.3    Watarai, M.4    Fukuda, I.5    Suzuki, T.6    Nakata, N.7    Komatsu, K.8    Yoshikawa, M.9    Sasakawa, C.10
  • 32
    • 34547886845 scopus 로고    scopus 로고
    • Site-specific modification of Shigella flexneri virF mRNA by tRNA-guanine transglycosylase in vitro
    • Hurt J.K., Olgen S., Garcia G.A. Site-specific modification of Shigella flexneri virF mRNA by tRNA-guanine transglycosylase in vitro. Nucleic Acids Res. 2007, 35:4905-4913.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4905-4913
    • Hurt, J.K.1    Olgen, S.2    Garcia, G.A.3
  • 33
    • 34250192588 scopus 로고    scopus 로고
    • Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding
    • Stengl B., Meyer E.A., Heine A., Brenk R., Diederich F., Klebe G. Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding. J. Mol. Biol. 2007, 370:492-511.
    • (2007) J. Mol. Biol. , vol.370 , pp. 492-511
    • Stengl, B.1    Meyer, E.A.2    Heine, A.3    Brenk, R.4    Diederich, F.5    Klebe, G.6
  • 34
    • 0037310429 scopus 로고    scopus 로고
    • Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA
    • Iwata-Reuyl D. Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA. Bioorg. Chem. 2003, 31:24-43.
    • (2003) Bioorg. Chem. , vol.31 , pp. 24-43
    • Iwata-Reuyl, D.1
  • 35
    • 84864396740 scopus 로고    scopus 로고
    • Biosynthesis of pyrrolopyrimidines
    • McCarty R.M., Bandarian V. Biosynthesis of pyrrolopyrimidines. Bioorg. Chem. 2012, 43:15-25.
    • (2012) Bioorg. Chem. , vol.43 , pp. 15-25
    • McCarty, R.M.1    Bandarian, V.2
  • 37
    • 0017459030 scopus 로고
    • Isolation of mammalian tRNAAsp and tRNATyr by lectin-Sepharose affinity column chromatography
    • Okada N., Shindo-Okada N., Nishimura S. Isolation of mammalian tRNAAsp and tRNATyr by lectin-Sepharose affinity column chromatography. Nucleic Acids Res. 1977, 4:415-423.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 415-423
    • Okada, N.1    Shindo-Okada, N.2    Nishimura, S.3
  • 42
    • 41649108068 scopus 로고    scopus 로고
    • Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria
    • Meyer M.M., Roth A., Chervin S.M., Garcia G.A., Breaker R.R. Confirmation of a second natural preQ1 aptamer class in Streptococcaceae bacteria. RNA 2008, 14:685-695.
    • (2008) RNA , vol.14 , pp. 685-695
    • Meyer, M.M.1    Roth, A.2    Chervin, S.M.3    Garcia, G.A.4    Breaker, R.R.5
  • 43
    • 84879103214 scopus 로고    scopus 로고
    • Structure of a class II preQ1 riboswitch reveals ligand recognition by a new fold
    • Liberman J.A., Salim M., Krucinska J., Wedekind J.E. Structure of a class II preQ1 riboswitch reveals ligand recognition by a new fold. Nat. Chem. Biol. 2013, 9:353-355.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 353-355
    • Liberman, J.A.1    Salim, M.2    Krucinska, J.3    Wedekind, J.E.4
  • 44
    • 84893843560 scopus 로고    scopus 로고
    • Structural determinants for ligand capture by a class II preQ1 riboswitch
    • Kang M., Eichhorn C.D., Feigon J. Structural determinants for ligand capture by a class II preQ1 riboswitch. Proc. Natl. Acad. Sci. U. S. A. 2014, 116:E663-E671.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.116 , pp. E663-E671
    • Kang, M.1    Eichhorn, C.D.2    Feigon, J.3
  • 45
    • 62549154008 scopus 로고    scopus 로고
    • Structural Insights into riboswitch control of the biosynthesis of queuosine, a modified nucleotide found in the anticodon of tRNA
    • (Erratum in: 2010, 2039, 2653-2655)
    • Kang M., Peterson R., Feigon J. Structural Insights into riboswitch control of the biosynthesis of queuosine, a modified nucleotide found in the anticodon of tRNA. Mol. Cell 2009, 33:784-790. (Erratum in: 2010, 2039, 2653-2655).
    • (2009) Mol. Cell , vol.33 , pp. 784-790
    • Kang, M.1    Peterson, R.2    Feigon, J.3
  • 46
    • 62049086072 scopus 로고    scopus 로고
    • Cocrystal structure of a class I preQ1 riboswitch reveals a pseudoknot recognizing an essential hypermodified nucleobase
    • Klein D.J., Edwards T.E., Ferre-D'Amare A.R. Cocrystal structure of a class I preQ1 riboswitch reveals a pseudoknot recognizing an essential hypermodified nucleobase. Nat. Struct. Mol. Biol. 2009, 16:343-344.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 343-344
    • Klein, D.J.1    Edwards, T.E.2    Ferre-D'Amare, A.R.3
  • 47
    • 66449089224 scopus 로고    scopus 로고
    • The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain
    • Spitale R.C., Torelli A.T., Krucinska J., Bandarian V., Wedekind J.E. The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain. J. Biol. Chem. 2009, 284:11012-11016.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11012-11016
    • Spitale, R.C.1    Torelli, A.T.2    Krucinska, J.3    Bandarian, V.4    Wedekind, J.E.5
  • 48
    • 79960114180 scopus 로고    scopus 로고
    • Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation
    • Jenkins J.L., Krucinska J., McCarty R.M., Bandarian V., Wedekind J.E. Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation. J. Biol. Chem. 2011, 286:24626-24637.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24626-24637
    • Jenkins, J.L.1    Krucinska, J.2    McCarty, R.M.3    Bandarian, V.4    Wedekind, J.E.5
  • 49
    • 67650445952 scopus 로고    scopus 로고
    • Evidence for pseudoknot formation of class I preQ1 riboswitch aptamers
    • Rieder U., Lang K., Kreutz C., Polacek N., Micura R. Evidence for pseudoknot formation of class I preQ1 riboswitch aptamers. Chembiochem 2009, 10:1141-1144.
    • (2009) Chembiochem , vol.10 , pp. 1141-1144
    • Rieder, U.1    Lang, K.2    Kreutz, C.3    Polacek, N.4    Micura, R.5
  • 50
    • 79953716261 scopus 로고    scopus 로고
    • Comparison of solution and crystal structures of preQ1 riboswitch reveals calcium-induced changes in conformation and dynamics
    • Zhang Q., Kang M., Peterson R.D., Feigon J. Comparison of solution and crystal structures of preQ1 riboswitch reveals calcium-induced changes in conformation and dynamics. J. Am. Chem. Soc. 2011, 133:5190-5193.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5190-5193
    • Zhang, Q.1    Kang, M.2    Peterson, R.D.3    Feigon, J.4
  • 51
    • 65649096161 scopus 로고    scopus 로고
    • Crystallization of the glmS ribozyme-riboswitch
    • Klein D.J., Ferre-D'Amare A.R. Crystallization of the glmS ribozyme-riboswitch. Methods Mol. Biol. 2009, 540:129-139.
    • (2009) Methods Mol. Biol. , vol.540 , pp. 129-139
    • Klein, D.J.1    Ferre-D'Amare, A.R.2
  • 52
    • 77954627972 scopus 로고    scopus 로고
    • Folding of a transcriptionally acting preQ1 riboswitch
    • Rieder U., Kreutz C., Micura R. Folding of a transcriptionally acting preQ1 riboswitch. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:10804-10809.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 10804-10809
    • Rieder, U.1    Kreutz, C.2    Micura, R.3
  • 53
    • 26444620938 scopus 로고    scopus 로고
    • The kinetics of ligand binding by an adenine-sensing riboswitch
    • Wickiser J.K., Cheah M.T., Breaker R.R., Crothers D.M. The kinetics of ligand binding by an adenine-sensing riboswitch. Biochemistry 2005, 44:13404-13414.
    • (2005) Biochemistry , vol.44 , pp. 13404-13414
    • Wickiser, J.K.1    Cheah, M.T.2    Breaker, R.R.3    Crothers, D.M.4
  • 54
    • 15944382675 scopus 로고    scopus 로고
    • The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch
    • Wickiser J.K., Winkler W.C., Breaker R.R., Crothers D.M. The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch. Mol. Cell 2005, 18:49-60.
    • (2005) Mol. Cell , vol.18 , pp. 49-60
    • Wickiser, J.K.1    Winkler, W.C.2    Breaker, R.R.3    Crothers, D.M.4
  • 55
    • 84865243362 scopus 로고    scopus 로고
    • Riboswitch structure in the ligand-free state, Wiley interdisciplinary reviews
    • Liberman J.A., Wedekind J.E. Riboswitch structure in the ligand-free state, Wiley interdisciplinary reviews. RNA 2012, 3:369-384.
    • (2012) RNA , vol.3 , pp. 369-384
    • Liberman, J.A.1    Wedekind, J.E.2
  • 57
    • 33646007627 scopus 로고    scopus 로고
    • An RNA sensor for intracellular Mg(2+)
    • Cromie M.J., Shi Y., Latifi T., Groisman E.A. An RNA sensor for intracellular Mg(2+). Cell 2006, 125:71-84.
    • (2006) Cell , vol.125 , pp. 71-84
    • Cromie, M.J.1    Shi, Y.2    Latifi, T.3    Groisman, E.A.4
  • 58
    • 33745635350 scopus 로고    scopus 로고
    • Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch
    • Serganov A., Polonskaia A., Phan A.T., Breaker R.R., Patel D.J. Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch. Nature 2006, 441:1167-1171.
    • (2006) Nature , vol.441 , pp. 1167-1171
    • Serganov, A.1    Polonskaia, A.2    Phan, A.T.3    Breaker, R.R.4    Patel, D.J.5
  • 59
    • 33744469562 scopus 로고    scopus 로고
    • Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand
    • Thore S., Leibundgut M., Ban N. Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand. Science 2006, 312:1208-1211.
    • (2006) Science , vol.312 , pp. 1208-1211
    • Thore, S.1    Leibundgut, M.2    Ban, N.3
  • 60
    • 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., Doniach S. Dissecting electrostatic screening, specific ion binding, and ligand binding in an energetic model for glycine riboswitch folding. RNA 2010, 16:708-719.
    • (2010) RNA , vol.16 , pp. 708-719
    • Lipfert, J.1    Sim, A.Y.2    Herschlag, D.3    Doniach, S.4
  • 63
    • 84867801144 scopus 로고    scopus 로고
    • Molecular mechanism of preQ1 riboswitch action: a molecular dynamics study
    • Banas P., Sklenovsky P., Wedekind J.E., Sponer J., Otyepka M. Molecular mechanism of preQ1 riboswitch action: a molecular dynamics study. J. Phys. Chem. B 2012, 116:12721-12734.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12721-12734
    • Banas, P.1    Sklenovsky, P.2    Wedekind, J.E.3    Sponer, J.4    Otyepka, M.5
  • 64
    • 84864185753 scopus 로고    scopus 로고
    • Pseudoknot preorganization of the preQ1 class I riboswitch
    • Santner T., Rieder U., Kreutz C., Micura R. Pseudoknot preorganization of the preQ1 class I riboswitch. J. Am. Chem. Soc. 2012, 134:11928-11931.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11928-11931
    • Santner, T.1    Rieder, U.2    Kreutz, C.3    Micura, R.4
  • 65
    • 84863405959 scopus 로고    scopus 로고
    • Unraveling the structural complexity in a single-stranded RNA tail: implications for efficient ligand binding in the prequeuosine riboswitch
    • Eichhorn C.D., Feng J., Suddala K.C., Walter N.G., Brooks C.L., Al-Hashimi H.M. Unraveling the structural complexity in a single-stranded RNA tail: implications for efficient ligand binding in the prequeuosine riboswitch. Nucleic Acids Res. 2012, 40:1345-1355.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1345-1355
    • Eichhorn, C.D.1    Feng, J.2    Suddala, K.C.3    Walter, N.G.4    Brooks, C.L.5    Al-Hashimi, H.M.6
  • 66
    • 79953060592 scopus 로고    scopus 로고
    • Cooperative and directional folding of the preQ1 riboswitch aptamer domain
    • Feng J., Walter N.G., Brooks C.L. Cooperative and directional folding of the preQ1 riboswitch aptamer domain. J. Am. Chem. Soc. 2011, 133:4196-4199.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4196-4199
    • Feng, J.1    Walter, N.G.2    Brooks, C.L.3
  • 67
    • 84866463347 scopus 로고    scopus 로고
    • Computational study of unfolding and regulation mechanism of preQ1 riboswitches
    • Gong Z., Zhao Y., Chen C., Xiao Y. Computational study of unfolding and regulation mechanism of preQ1 riboswitches. PLoS One 2012, 7:e45239.
    • (2012) PLoS One , vol.7 , pp. e45239
    • Gong, Z.1    Zhao, Y.2    Chen, C.3    Xiao, Y.4
  • 68
    • 84883281341 scopus 로고    scopus 로고
    • Protonation of trimethylamine N-oxide (TMAO) is required for stabilization of RNA tertiary structure
    • Denning E.J., Thirumalai D., MacKerell A.D. Protonation of trimethylamine N-oxide (TMAO) is required for stabilization of RNA tertiary structure. Biophys. Chem. 2013, 184:8-16.
    • (2013) Biophys. Chem. , vol.184 , pp. 8-16
    • Denning, E.J.1    Thirumalai, D.2    MacKerell, A.D.3
  • 69
    • 84882246260 scopus 로고    scopus 로고
    • Urea-induced denaturation of preQ1-riboswitch
    • Yoon J., Thirumalai D., Hyeon C. Urea-induced denaturation of preQ1-riboswitch. J. Am. Chem. Soc. 2013, 135:12112-12121.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12112-12121
    • Yoon, J.1    Thirumalai, D.2    Hyeon, C.3
  • 70
    • 0041620358 scopus 로고    scopus 로고
    • PSEUDOVIEWER2: visualization of RNA pseudoknots of any type
    • Han K., Byun Y. PSEUDOVIEWER2: visualization of RNA pseudoknots of any type. Nucleic Acids Res. 2003, 31:3432-3440.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3432-3440
    • Han, K.1    Byun, Y.2
  • 71
    • 14644435818 scopus 로고    scopus 로고
    • Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function
    • Theimer C.A., Blois C.A., Feigon J. Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function. Mol. Cell 2005, 17:671-682.
    • (2005) Mol. Cell , vol.17 , pp. 671-682
    • Theimer, C.A.1    Blois, C.A.2    Feigon, J.3
  • 72
    • 78649422018 scopus 로고    scopus 로고
    • Poly(A) tail recognition by a viral RNA element through assembly of a triple helix
    • Mitton-Fry R.M., DeGregorio S.J., Wang J., Steitz T.A., Steitz J.A. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. Science 2010, 330:1244-1247.
    • (2010) Science , vol.330 , pp. 1244-1247
    • Mitton-Fry, R.M.1    DeGregorio, S.J.2    Wang, J.3    Steitz, T.A.4    Steitz, J.A.5
  • 74
    • 71249121480 scopus 로고    scopus 로고
    • Aptamers and riboswitches: perspectives in biotechnology
    • Weigand J.E., Suess B. Aptamers and riboswitches: perspectives in biotechnology. Appl. Microbiol. Biotechnol. 2009, 85:229-236.
    • (2009) Appl. Microbiol. Biotechnol. , vol.85 , pp. 229-236
    • Weigand, J.E.1    Suess, B.2
  • 75
    • 84863617223 scopus 로고    scopus 로고
    • Engineered riboswitches: expanding researchers' toolbox with synthetic RNA regulators
    • Wittmann A., Suess B. Engineered riboswitches: expanding researchers' toolbox with synthetic RNA regulators. FEBS Lett. 2012, 586:2076-2083.
    • (2012) FEBS Lett. , vol.586 , pp. 2076-2083
    • Wittmann, A.1    Suess, B.2
  • 76
    • 84876532777 scopus 로고    scopus 로고
    • Exploiting preQ(1) riboswitches to regulate ribosomal frameshifting
    • Yu C.H., Luo J., Iwata-Reuyl D., Olsthoorn R.C. Exploiting preQ(1) riboswitches to regulate ribosomal frameshifting. ACS Chem. Biol. 2013, 8:733-740.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 733-740
    • Yu, C.H.1    Luo, J.2    Iwata-Reuyl, D.3    Olsthoorn, R.C.4
  • 77
    • 33845700514 scopus 로고    scopus 로고
    • Riboswitches as antibacterial drug targets
    • Blount K.F., Breaker R.R. Riboswitches as antibacterial drug targets. Nat. Biotechnol. 2006, 24:1558-1564.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1558-1564
    • Blount, K.F.1    Breaker, R.R.2
  • 78
    • 80053041142 scopus 로고    scopus 로고
    • Riboswitches: discovery of drugs that target bacterial gene-regulatory RNAs
    • Deigan K.E., Ferre-D'Amare A.R. Riboswitches: discovery of drugs that target bacterial gene-regulatory RNAs. Acc. Chem. Res. 2011, 44:1329-1338.
    • (2011) Acc. Chem. Res. , vol.44 , pp. 1329-1338
    • Deigan, K.E.1    Ferre-D'Amare, A.R.2
  • 83
    • 77950798696 scopus 로고    scopus 로고
    • Aptamer-controlled biofuel cells in logic systems and used as self-powered and intelligent logic aptasensors
    • Zhou M., Du Y., Chen C., Li B., Wen D., Dong S., Wang E. Aptamer-controlled biofuel cells in logic systems and used as self-powered and intelligent logic aptasensors. J. Am. Chem. Soc. 2010, 132:2172-2174.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2172-2174
    • Zhou, M.1    Du, Y.2    Chen, C.3    Li, B.4    Wen, D.5    Dong, S.6    Wang, E.7
  • 86
    • 84885929738 scopus 로고    scopus 로고
    • Theophylline-dependent riboswitch as a novel genetic tool for strict regulation of protein expression in cyanobacterium Synechococcus elongatus PCC 7942
    • Nakahira Y., Ogawa A., Asano H., Oyama T., Tozawa Y. Theophylline-dependent riboswitch as a novel genetic tool for strict regulation of protein expression in cyanobacterium Synechococcus elongatus PCC 7942. Plant Cell Physiol. 2013, 54:1724-1735.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 1724-1735
    • Nakahira, Y.1    Ogawa, A.2    Asano, H.3    Oyama, T.4    Tozawa, Y.5
  • 87
    • 0035010211 scopus 로고    scopus 로고
    • Geometric nomenclature and classification of RNA base pairs
    • Leontis N.B., Westhof E. Geometric nomenclature and classification of RNA base pairs. RNA 2001, 7:499-512.
    • (2001) RNA , vol.7 , pp. 499-512
    • Leontis, N.B.1    Westhof, E.2


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