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Volumn , Issue SUPPL. 34, 2008, Pages

RNA intramolecular dynamics by single-molecule FRET

Author keywords

Dynamics; Fluorescence resonance energy transfer (FRET); Fluorescent dyes; Nucleotide modifications; RNA folding; Single molecule; Splint ligation

Indexed keywords

BIOTIN; CYANINE DYE 3; CYANINE DYE 5; DEOXYRIBONUCLEOTIDE; FLUORESCEIN; FLUORESCENT DYE; OLIGORIBONUCLEOTIDE; PHOSPHORAMIDOUS ACID DERIVATIVE; TETRAMETHYLRHODAMINE;

EID: 58849135321     PISSN: 19349270     EISSN: 19349289     Source Type: Journal    
DOI: 10.1002/0471142700.nc1112s34     Document Type: Review
Times cited : (17)

References (51)
  • 1
    • 41449108157 scopus 로고    scopus 로고
    • An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments
    • Aitken, C.E., Marshall, R.A., and Puglisi, J.D. 2007. An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments. Biophys. J. 94:1826-1835.
    • (2007) Biophys. J. , vol.94 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 3
    • 0031463467 scopus 로고    scopus 로고
    • Ion-induced folding of the hammerhead ribozyme: A fluorescence resonance energy transfer study
    • Bassi, G.S., Murchie, A.I., Walter, F., Clegg, R.M., and Lilley, D.M. 1997. Ion-induced folding of the hammerhead ribozyme: A fluorescence resonance energy transfer study. EMBO J. 16:7481-7489.
    • (1997) EMBO J. , vol.16 , pp. 7481-7489
    • Bassi, G.S.1    Murchie, A.I.2    Walter, F.3    Clegg, R.M.4    Lilley, D.M.5
  • 4
    • 0033582291 scopus 로고    scopus 로고
    • Intra-tRNA distance measurements for nucleocapsid proteindependent tRNA unwinding during priming of HIV reverse transcription
    • Chan, B.,Weidemaier, K., Yip, W.T., Barbara, P.F., and Musier-Forsyth, K. 1999. Intra-tRNA distance measurements for nucleocapsid proteindependent tRNA unwinding during priming of HIV reverse transcription. Proc. Natl. Acad. Sci. U.S.A. 96:459-464.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 459-464
    • Chan, B.1    Weidemaier, K.2    Yip, W.T.3    Barbara, P.F.4    Musier-Forsyth, K.5
  • 5
    • 0026687952 scopus 로고
    • Fluorescence resonance energy transfer and nucleic acids
    • Clegg, R.M. 1992. Fluorescence resonance energy transfer and nucleic acids. Methods Enzymol. 211:353-388.
    • (1992) Methods Enzymol. , vol.211 , pp. 353-388
    • Clegg, R.M.1
  • 6
    • 33744797914 scopus 로고    scopus 로고
    • Conformational heterogeneity in RNA polymerase observed by single-pair FRET microscopy
    • Coban, O., Lamb, D.C., Zaychikov, E., Heumann, H., and Nienhaus, G.U. 2006. Conformational heterogeneity in RNA polymerase observed by single-pair FRET microscopy. Biophys. J. 90:4605-4617.
    • (2006) Biophys. J. , vol.90 , pp. 4605-4617
    • Coban, O.1    Lamb, D.C.2    Zaychikov, E.3    Heumann, H.4    Nienhaus, G.U.5
  • 7
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Forster distance dependence and subpopulations
    • Deniz, A.A., Dahan, M., Grunwell, J.R., Ha, T., Faulhaber, A.E., Chemla, D.S., Weiss, S., and Schultz, P.G. 1999. Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Forster distance dependence and subpopulations. Proc. Natl. Acad. Sci. U.S.A. 96:3670-3675.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 8
    • 0036180593 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) and competing processes in donoracceptor substituted DNA strands: A comparative study of ensemble and single-molecule data
    • Dietrich, A., Buschmann, V., Müller, C., and Sauer, M. 2002. Fluorescence resonance energy transfer (FRET) and competing processes in donoracceptor substituted DNA strands: A comparative study of ensemble and single-molecule data. J. Biotechnol. 82:211-231.
    • (2002) J. Biotechnol. , vol.82 , pp. 211-231
    • Dietrich, A.1    Buschmann, V.2    Müller, C.3    Sauer, M.4
  • 9
    • 1842607369 scopus 로고    scopus 로고
    • Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allowreversible folding of immobilized proteins
    • Groll, J., Amirgoulova, E.V., Ameringer, T., Heyes, C.D., Röcker, C., Nienhaus, G.U., and Möller, M. 2004. Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allowreversible folding of immobilized proteins. J. Am. Chem. Soc. 126:4234-4239.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4234-4239
    • Groll, J.1    Amirgoulova, E.V.2    Ameringer, T.3    Heyes, C.D.4    Röcker, C.5    Nienhaus, G.U.6    Möller, M.7
  • 10
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha, T., Enderle, T., Ogletree, D.F., Chemla, D.S., Selvin, P.R., and Weiss, S. 1996. Probing the interaction between two single molecules: Fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl. Acad. Sci. U.S.A. 93:6264-6268.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Ogletree, D.F.3    Chemla, D.S.4    Selvin, P.R.5    Weiss, S.6
  • 12
    • 4444316252 scopus 로고    scopus 로고
    • Biocompatible surfaces for specific tethering of individual protein molecules
    • Heyes, C.D., Kobitski, A.Y., and Nienhaus, G.U. 2004. Biocompatible surfaces for specific tethering of individual protein molecules. J. Phys. Chem. B 108:13387-13394.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 13387-13394
    • Heyes, C.D.1    Kobitski, A.Y.2    Nienhaus, G.U.3
  • 13
    • 34249681351 scopus 로고    scopus 로고
    • Synthesis patterning and applications of star-shaped poly(ethylene glycol) biofunctionalized surfaces
    • Heyes, C.D., Groll, J., Möller, M., and Nienhaus, G.U. 2007. Synthesis, patterning and applications of star-shaped poly(ethylene glycol) biofunctionalized surfaces. Mol. Biosyst. 3:419-430.
    • (2007) Mol. Biosyst. , vol.3 , pp. 419-430
    • Heyes, C.D.1    Groll, J.2    Möller, M.3    Nienhaus, G.U.4
  • 14
    • 20444373042 scopus 로고    scopus 로고
    • Direct observation of delayed fluorescence from a remarkable back-isomerization in Cy5
    • Huang, Z., Ji, D., Xia, A.D., Koberling, F., Patting, M., and Erdmann, R. 2005. Direct observation of delayed fluorescence from a remarkable back-isomerization in Cy5. J. Am. Chem. Soc. 127:8064-8066.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8064-8066
    • Huang, Z.1    Ji, D.2    Xia, A.D.3    Koberling, F.4    Patting, M.5    Erdmann, R.6
  • 15
    • 0033413080 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution
    • Ishii, Y., Yoshida, T., Funatsu, T., Wazawa, T., and Yanagida, T. 1999. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys. 247:163-173.
    • (1999) Chem. Phys. , vol.247 , pp. 163-173
    • Ishii, Y.1    Yoshida, T.2    Funatsu, T.3    Wazawa, T.4    Yanagida, T.5
  • 17
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • Kapanidis, A.N., Lee, N.K., Laurence, T.A., Doose, S., Margeat, E., and Weiss, S. 2004. Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules. Proc. Natl. Acad. Sci. U.S.A. 101:8936-8941.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5    Weiss, S.6
  • 18
    • 0037006790 scopus 로고    scopus 로고
    • Mg2+- dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
    • Kim, H.D., Nienhaus, G.U., Ha, T., Orr, J.W., Williamson, J.R., and Chu, S. 2002. Mg2+- dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules. Proc.Natl. Acad. Sci. U.S.A. 99:4284-4289.
    • (2002) Proc.Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4284-4289
    • Kim, H.D.1    Nienhaus, G.U.2    Ha, T.3    Orr, J.W.4    Williamson, J.R.5    Chu, S.6
  • 19
    • 0035909052 scopus 로고    scopus 로고
    • Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif
    • Klostermeier, D. and Millar, D.P. 2001. Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif. Biochemistry 40:11211-11218.
    • (2001) Biochemistry , vol.40 , pp. 11211-11218
    • Klostermeier, D.1    Millar, D.P.2
  • 20
    • 34247848007 scopus 로고    scopus 로고
    • Mg2+-dependent folding of a Diels-Alderase ribozyme probed by single-molecule FRET analysis
    • Kobitski, A.Y., Nierth, A., Helm, M., Jäschke, A., and Nienhaus, G.U. 2007. Mg2+-dependent folding of a Diels-Alderase ribozyme probed by single-molecule FRET analysis. Nucleic Acids Res. 35:2047-2059.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2047-2059
    • Kobitski, A.Y.1    Nierth, A.2    Helm, M.3    Jäschke, A.4    Nienhaus, G.U.5
  • 21
    • 28344451166 scopus 로고    scopus 로고
    • Optimizing splinted ligation of highly structured small RNAs
    • Kurschat, W.C., Muller, J., Wombacher, R., and Helm, M. 2005. Optimizing splinted ligation of highly structured small RNAs. RNA 11:1909-1914.
    • (2005) RNA , vol.11 , pp. 1909-1914
    • Kurschat, W.C.1    Muller, J.2    Wombacher, R.3    Helm, M.4
  • 22
    • 27344452885 scopus 로고    scopus 로고
    • Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions
    • Kuzmenkina, E.V., Heyes, C.D., and Nienhaus, G.U. 2005. Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions. Proc. Natl. Acad. Sci. U.S.A. 102:15471-15476.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15471-15476
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 24
    • 37849026396 scopus 로고    scopus 로고
    • Folding of 8-17 deoxyribozyme studied by three-color alternating-laser excitation of single molecules
    • Lee, N.K., Koh, H.R., Han, K.Y., and Kim, S.K. 2007. Folding of 8-17 deoxyribozyme studied by three-color alternating-laser excitation of single molecules. J. Am. Chem. Soc. 129:15526-15534.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15526-15534
    • Lee, N.K.1    Koh, H.R.2    Han, K.Y.3    Kim, S.K.4
  • 27
    • 0032061318 scopus 로고    scopus 로고
    • Folding of the hairpin ribozyme in its natural conformation achieves close physical proximity of the loops
    • Murchie, A.I., Thomson, J.B.,Walter, F., and Lilley, D.M. 1998. Folding of the hairpin ribozyme in its natural conformation achieves close physical proximity of the loops. Mol. Cell 1:873-881.
    • (1998) Mol. Cell , vol.1 , pp. 873-881
    • Murchie, A.I.1    Thomson, J.B.2    Walter, F.3    Lilley, D.M.4
  • 28
    • 33845273835 scopus 로고    scopus 로고
    • Exploring protein structure and dynamics under denaturing conditions by single-molecule FRET analysis
    • Nienhaus, G.U. 2006. Exploring protein structure and dynamics under denaturing conditions by single-molecule FRET analysis. Macromol. Biosci. 6:907-922.
    • (2006) Macromol. Biosci. , vol.6 , pp. 907-922
    • Nienhaus, G.U.1
  • 31
    • 0032824909 scopus 로고    scopus 로고
    • Site-specific labeling of RNA with fluorophores and other structural probes
    • Qin, P.Z. and Pyle, A.M. 1999. Site-specific labeling of RNA with fluorophores and other structural probes. Methods 18:60-70.
    • (1999) Methods , vol.18 , pp. 60-70
    • Qin, P.Z.1    Pyle, A.M.2
  • 32
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and orientations: Much to FRET about?
    • Rasnik, I., McKinney, S.A., and Ha. T. 2005. Surfaces and orientations: Much to FRET about? Acc. Chem. Res. 38:542-548.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 33
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long-lasting single-molecule fluorescence imaging
    • Rasnik, I., McKinney, S.A., and Ha, T. 2006. Nonblinking and long-lasting single-molecule fluorescence imaging. Nat. Methods 3:891-893.
    • (2006) Nat. Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 35
    • 22944457862 scopus 로고    scopus 로고
    • Using fluorescence resonance energy transfer to measure distances along individual DNA molecules: Corrections due to nonideal transfer
    • Sabanayagam, C.R., Eid, J.S., and Meller, A. 2005. Using fluorescence resonance energy transfer to measure distances along individual DNA molecules: Corrections due to nonideal transfer. J. Chem. Phys. 122:061103.
    • (2005) J. Chem. Phys. , vol.122 , pp. 061103
    • Sabanayagam, C.R.1    Eid, J.S.2    Meller, A.3
  • 36
    • 0032545045 scopus 로고    scopus 로고
    • Novel RNA synthesis method using 5′-Silyl-2′-Orthoester protecting groups
    • Scaringe, S.A., Wincott, F.E., and Caruthers, M.H. 1998. Novel RNA synthesis method using 5′-Silyl-2′-Orthoester protecting groups. J. Am. Chem. Soc. 120:11820-11821.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11820-11821
    • Scaringe, S.A.1    Wincott, F.E.2    Caruthers, M.H.3
  • 37
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P.R. 2000. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7:730-734.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 38
    • 0032834899 scopus 로고    scopus 로고
    • Rapid kinetic characterization of hammerhead ribozymes by real-time monitoring of fluorescence resonance energy transfer (FRET)
    • Singh, K.K., Parwaresch, R., and Krupp, G. 1999. Rapid kinetic characterization of hammerhead ribozymes by real-time monitoring of fluorescence resonance energy transfer (FRET). RNA 5:1348-1356.
    • (1999) RNA , vol.5 , pp. 1348-1356
    • Singh, K.K.1    Parwaresch, R.2    Krupp, G.3
  • 39
  • 41
    • 0024457555 scopus 로고
    • Synthesis and characterization of DNA oligomers and duplexes containing covalently attached molecular labels: Comparison of biotin, fluorescein, and pyrene labels by thermodynamic and optical spectroscopic measurements
    • Telser, J., Cruickshank, K.A., Morrison, L.E., and Netzel, T.L. 1989. Synthesis and characterization of DNA oligomers and duplexes containing covalently attached molecular labels: Comparison of biotin, fluorescein, and pyrene labels by thermodynamic and optical spectroscopic measurements. J. Am. Chem. Soc. 111:6966.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6966
    • Telser, J.1    Cruickshank, K.A.2    Morrison, L.E.3    Netzel, T.L.4
  • 42
    • 0027973506 scopus 로고
    • A three-dimensional model for the hammerhead ribozyme based on fluorescence measurements
    • Tuschl, T., Gohlke, C., Jovin, T.M.,Westhof, E., and Eckstein, F. 1994. A three-dimensional model for the hammerhead ribozyme based on fluorescence measurements. Science 266:785-789.
    • (1994) Science , vol.266 , pp. 785-789
    • Tuschl, T.1    Gohlke, C.2    Jovin, T.M.3    Westhof, E.4    Eckstein, F.5
  • 44
    • 0028929659 scopus 로고
    • Identification of bases in 16S rRNAessential for tRNAbinding at the 30S ribosomal P site
    • von Ahsen, U. and Noller, H.F. 1995. Identification of bases in 16S rRNAessential for tRNAbinding at the 30S ribosomal P site. Science 267:234-237.
    • (1995) Science , vol.267 , pp. 234-237
    • von Ahsen, U.1    Noller, H.F.2
  • 45
    • 0032522574 scopus 로고    scopus 로고
    • Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer
    • Walter, N.G., Hampel, K.J., Brown, K.M., and Burke, J.M. 1998. Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer. EMBO J. 17:2378-2391.
    • (1998) EMBO J. , vol.17 , pp. 2378-2391
    • Walter, N.G.1    Hampel, K.J.2    Brown, K.M.3    Burke, J.M.4
  • 46
    • 0032979707 scopus 로고    scopus 로고
    • Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction
    • Walter, N.G., Burke, J.M., and Millar, D.P. 1999. Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction. Nat. Struct. Biol. 6:544-549.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 544-549
    • Walter, N.G.1    Burke, J.M.2    Millar, D.P.3
  • 47
    • 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
  • 48
    • 0035957060 scopus 로고    scopus 로고
    • A base change in the catalytic core of the hairpin ribozyme perturbs function but not domain docking
    • Walter, N.G., Chan, P.A., Hampel, K.J., Millar, D.P., and Burke, J.M. 2001. A base change in the catalytic core of the hairpin ribozyme perturbs function but not domain docking. Biochemistry 40:2580-2587.
    • (2001) Biochemistry , vol.40 , pp. 2580-2587
    • Walter, N.G.1    Chan, P.A.2    Hampel, K.J.3    Millar, D.P.4    Burke, J.M.5
  • 49
    • 0033702974 scopus 로고    scopus 로고
    • Characterization of photo-induced isomerization and backisomerization of the cyanine dye Cy5 by fluorescence correlation spectroscopy
    • Widengren, J. and Schwille, P. 2000. Characterization of photo-induced isomerization and backisomerization of the cyanine dye Cy5 by fluorescence correlation spectroscopy. J. Phys. Chem. 104:6416-6428.
    • (2000) J. Phys. Chem. , vol.104 , pp. 6416-6428
    • Widengren, J.1    Schwille, P.2
  • 51
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang, X., Kim, H., Pereira, M.J., Babcock, H.P., Walter, N.G., and Chu, S. 2002. Correlating structural dynamics and function in single ribozyme molecules. Science 296:1473-1476.
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.1    Kim, H.2    Pereira, M.J.3    Babcock, H.P.4    Walter, N.G.5    Chu, S.6


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