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Volumn 44, Issue 26, 2005, Pages 9348-9358

The procapsid binding domain of φ29 packaging RNA has a modular architecture and requires 2′-hydroxyl groups in packaging RNA interaction

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING ENERGY; COMPLEXATION; DIMERS; DNA; GENETIC ENGINEERING; MOLECULAR DYNAMICS; MONOMERS; MUTAGENESIS;

EID: 21644486473     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0475020     Document Type: Article
Times cited : (19)

References (70)
  • 1
    • 0024452966 scopus 로고
    • DNA packaging in dsDNA bacteriophages
    • Black, L. W. (1989) DNA packaging in dsDNA bacteriophages, Annu. Rev. Microbiol. 43, 267-292.
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 267-292
    • Black, L.W.1
  • 2
    • 0028000731 scopus 로고
    • Structure of viral connectors and their function in bacteriophage assembly and DNA packaging
    • Valpuesta, J. M., and Carrascosa, J. L. (1994) Structure of viral connectors and their function in bacteriophage assembly and DNA packaging, Q. Rev. Biophys. 27, 107-155.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 107-155
    • Valpuesta, J.M.1    Carrascosa, J.L.2
  • 3
    • 0031218420 scopus 로고    scopus 로고
    • Phage DNA packaging
    • Fujisawa, H., and Morita, M. (1997) Phage DNA packaging, Genes Cells 2, 537-545.
    • (1997) Genes Cells , vol.2 , pp. 537-545
    • Fujisawa, H.1    Morita, M.2
  • 4
    • 0033966457 scopus 로고    scopus 로고
    • The terminase enzyme from bacteriophage lambda: A DNA-packaging machine
    • Catalano, C. E. (2000) The terminase enzyme from bacteriophage lambda: a DNA-packaging machine, Cell. Mol. Life Sci. 57, 128-148.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 128-148
    • Catalano, C.E.1
  • 6
    • 0036043690 scopus 로고    scopus 로고
    • Structure and function of φ29 hexameric RNA that drives the viral DNA packaging motor: Review
    • Quo, P. (2002) Structure and function of φ29 hexameric RNA that drives the viral DNA packaging motor: Review, Prog. Nucleic Acids Res. Mol. Biol. 72, 415-473.
    • (2002) Prog. Nucleic Acids Res. Mol. Biol. , vol.72 , pp. 415-473
    • Quo, P.1
  • 7
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage phi29 portal motor can package DNA against a large internal force
    • Smith, D. E., Tans, S. J., Smith, S. B., Grimes, S., Anderson, D. L., and Bustamante, C. (2001) The bacteriophage phi29 portal motor can package DNA against a large internal force, Nature 413, 748-752.
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 8
    • 0030896203 scopus 로고    scopus 로고
    • Sequential action of six DNA-packing pRNAs during phage φ29 genomic DNA translocation
    • Chen, C., and Guo, P. (1997) Sequential action of six DNA-packing pRNAs during phage φ29 genomic DNA translocation, J. Virol. 71, 3864-3871.
    • (1997) J. Virol. , vol.71 , pp. 3864-3871
    • Chen, C.1    Guo, P.2
  • 10
    • 0036301072 scopus 로고    scopus 로고
    • Detailed architecture of a DNA translocating machine: The high-resolution structure of the bacteriophage phi29 connector particle
    • Guasch, A., Pous, J., Ibarra, B., Gomis-Ruth, F. X., Valpuesta, J. M., Sousa, N., Carrascosa, J. L., and Coll, M. (2002) Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle, J. Mol. Biol. 315, 663-676.
    • (2002) J. Mol. Biol. , vol.315 , pp. 663-676
    • Guasch, A.1    Pous, J.2    Ibarra, B.3    Gomis-Ruth, F.X.4    Valpuesta, J.M.5    Sousa, N.6    Carrascosa, J.L.7    Coll, M.8
  • 11
    • 0037339538 scopus 로고    scopus 로고
    • Models of bacteriophage DNA packaging motors
    • Serwer, P. (2003) Models of bacteriophage DNA packaging motors, J. Struct. Biol. 141, 179-188.
    • (2003) J. Struct. Biol. , vol.141 , pp. 179-188
    • Serwer, P.1
  • 12
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage φ29 DNA
    • Guo, P., Erickson, S., and Anderson, D. (1987) A small viral RNA is required for in vitro packaging of bacteriophage φ29 DNA, Science 236, 690-694.
    • (1987) Science , vol.236 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 13
    • 0028175938 scopus 로고
    • Identification of bacteriophage φ29 prohead RNA domains necessary for in vitro DNA-gp3 packaging
    • Reid, R. J. D., Zhang, F., Benson, S., and Anderson, D. (1994) Identification of bacteriophage φ29 prohead RNA domains necessary for in vitro DNA-gp3 packaging, J. Biol. Chem. 269, 9084-9089.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9084-9089
    • Reid, R.J.D.1    Zhang, F.2    Benson, S.3    Anderson, D.4
  • 14
    • 0028361637 scopus 로고
    • The proximate 5′ and 3′ ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage φ29 DNA
    • Zhang, C. L., Lee, C.-S., and Guo, P. (1994) The proximate 5′ and 3′ ends of the 120-base viral RNA (pRNA) are crucial for the packaging of bacteriophage φ29 DNA, Virology 201, 77-85.
    • (1994) Virology , vol.201 , pp. 77-85
    • Zhang, C.L.1    Lee, C.-S.2    Guo, P.3
  • 15
    • 0027992332 scopus 로고
    • Characterization of the prohead-pRNA interaction of bacteriophage φ29
    • Reid, R. J. D., Bodley, J. W., and Anderson, D. (1994) Characterization of the prohead-pRNA interaction of bacteriophage φ29, J. Biol. Chem. 269, 5157-5162.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5157-5162
    • Reid, R.J.D.1    Bodley, J.W.2    Anderson, D.3
  • 16
    • 0028358819 scopus 로고
    • Probing the structure of the bacteriophage φ29 prohead RNA with specific mutations
    • Reid, R. J. D., Zhange, F., Benson, S., and Anderson, D. (1994) Probing the structure of the bacteriophage φ29 prohead RNA with specific mutations, J. Biol. Chem. 269, 18656-18661.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18656-18661
    • Reid, R.J.D.1    Zhange, F.2    Benson, S.3    Anderson, D.4
  • 17
    • 0030817119 scopus 로고    scopus 로고
    • Boundary of pRNA functional domains and minimum pRNA sequence requirement for specific connector binding and DNA packaging of phage φ29
    • Garver, K., and Guo, P. (1997) Boundary of pRNA functional domains and minimum pRNA sequence requirement for specific connector binding and DNA packaging of phage φ29, RNA 3, 1068-1079.
    • (1997) RNA , vol.3 , pp. 1068-1079
    • Garver, K.1    Guo, P.2
  • 18
    • 0032110708 scopus 로고    scopus 로고
    • Inter-RNA interaction of phage φ29 pRNA to form a hexameric complex for viral DNA transportation
    • Guo, P., Zhang, C., Chen, C., Garver, K., and Trottier, M. (1998) Inter-RNA interaction of phage φ29 pRNA to form a hexameric complex for viral DNA transportation, Mol. Cell 2, 149-155.
    • (1998) Mol. Cell , vol.2 , pp. 149-155
    • Guo, P.1    Zhang, C.2    Chen, C.3    Garver, K.4    Trottier, M.5
  • 20
    • 0032981057 scopus 로고    scopus 로고
    • Sequence requirement for hand-in-hand interaction in formation of pRNA dimers and hexamers to gear phi29 DNA translocation motor
    • Chen, C. P., Zhang, C. L., and Guo, P. (1999) Sequence requirement for hand-in-hand interaction in formation of pRNA dimers and hexamers to gear phi29 DNA translocation motor, RNA 5, 805-818.
    • (1999) RNA , vol.5 , pp. 805-818
    • Chen, C.P.1    Zhang, C.L.2    Guo, P.3
  • 21
    • 0033834945 scopus 로고    scopus 로고
    • Probing the structure of the monomers and dimers of the bacterial virus phi29 hexamer RNA complex by chemical modification
    • Trottier, M., Mat-Arip, Y., Zhang, C. L., Chen, C. P., Sheng, S., Shao, Z., and Guo, P. (2000) Probing the structure of the monomers and dimers of the bacterial virus phi29 hexamer RNA complex by chemical modification, RNA 6, 1-10.
    • (2000) RNA , vol.6 , pp. 1-10
    • Trottier, M.1    Mat-Arip, Y.2    Zhang, C.L.3    Chen, C.P.4    Sheng, S.5    Shao, Z.6    Guo, P.7
  • 22
    • 0034625371 scopus 로고    scopus 로고
    • Dimer as a building block in assembling RNA
    • Chen, C. P., Sheng, S., Shao, Z., and Guo, P. (2000) Dimer as a building block in assembling RNA, J. Biol. Chem. 275, 17510-17516.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17510-17516
    • Chen, C.P.1    Sheng, S.2    Shao, Z.3    Guo, P.4
  • 23
    • 0037036444 scopus 로고    scopus 로고
    • Computer modeling of three-dimensional structure of DNA-packaging RNA (pRNA) monomer, dimer, and hexamer of phi29 DNA packaging motor
    • Hoeprich, S., and Guo, P. (2002) Computer modeling of three-dimensional structure of DNA-packaging RNA (pRNA) monomer, dimer, and hexamer of phi29 DNA packaging motor, J. Biol. Chem. 23, 20794-20804.
    • (2002) J. Biol. Chem. , vol.23 , pp. 20794-20804
    • Hoeprich, S.1    Guo, P.2
  • 24
    • 0034685605 scopus 로고    scopus 로고
    • Topology of the components of the DNA packaging machinery in the phage φ29 prohead
    • Ibarra, B., Gaston, J. R., Llorca, O., Valle, M., Valpuesta, J. M., and Carrascosa, J. L. (2000) Topology of the components of the DNA packaging machinery in the phage φ29 prohead, J. Mol. Biol. 298, 807-815.
    • (2000) J. Mol. Biol. , vol.298 , pp. 807-815
    • Ibarra, B.1    Gaston, J.R.2    Llorca, O.3    Valle, M.4    Valpuesta, J.M.5    Carrascosa, J.L.6
  • 25
    • 0025028872 scopus 로고
    • RNA dependence of the bacteriophage phi29 DNA packaging ATPase
    • Grimes, S., and Anderson, D. (1990) RNA dependence of the bacteriophage phi29 DNA packaging ATPase, J. Mol. Biol. 215, 559-566.
    • (1990) J. Mol. Biol. , vol.215 , pp. 559-566
    • Grimes, S.1    Anderson, D.2
  • 26
    • 0037470196 scopus 로고    scopus 로고
    • A viral RNA that binds ATP and contains a motif similar to an ATP-binding aptamer from SELEX
    • Shu, D., and Guo, P. (2003) A viral RNA that binds ATP and contains a motif similar to an ATP-binding aptamer from SELEX, J. Biol. Chem. 278, 7119-7125.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7119-7125
    • Shu, D.1    Guo, P.2
  • 27
    • 0042172858 scopus 로고    scopus 로고
    • Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus
    • Hoeprich, S., Zhou, Q., Guo, S., Shu, D., Qi, G., Wang, Y., and Guo, P. (2003) Bacterial virus phi29 pRNA as a hammerhead ribozyme escort to destroy hepatitis B virus, Gene Ther. 10, 1258-1267.
    • (2003) Gene Ther. , vol.10 , pp. 1258-1267
    • Hoeprich, S.1    Zhou, Q.2    Guo, S.3    Shu, D.4    Qi, G.5    Wang, Y.6    Guo, P.7
  • 28
    • 4644326818 scopus 로고    scopus 로고
    • Bottom-up assembly of RNA arrays and superstructures as potential parts in nanotechnology
    • Shu, D., Moll, W., Deng, Z., Mao, C., and Guo, P. (2004) Bottom-up assembly of RNA arrays and superstructures as potential parts in nanotechnology, Nano Lett. 4, 1717-1723.
    • (2004) Nano Lett. , vol.4 , pp. 1717-1723
    • Shu, D.1    Moll, W.2    Deng, Z.3    Mao, C.4    Guo, P.5
  • 29
    • 2342493879 scopus 로고    scopus 로고
    • Construction of phi29 DNA-packaging RNA monomers, dimers, and trimers with variable sizes and shapes as potential parts for nanodevices
    • Shu, D., Huang, L. P., Hoeprich, S., and Guo, P. (2003) Construction of phi29 DNA-packaging RNA monomers, dimers, and trimers with variable sizes and shapes as potential parts for nanodevices, J. Nanosci. Nanotechnol. 3, 295-302.
    • (2003) J. Nanosci. Nanotechnol. , vol.3 , pp. 295-302
    • Shu, D.1    Huang, L.P.2    Hoeprich, S.3    Guo, P.4
  • 30
    • 0031060313 scopus 로고    scopus 로고
    • 2+-induced conformational change of packaging RNA for procapsid recognition and binding during phage φ29 DNA encaspsidation
    • 2+-induced conformational change of packaging RNA for procapsid recognition and binding during phage φ29 DNA encaspsidation, J. Virol. 71, 495-500.
    • (1997) J. Virol. , vol.71 , pp. 495-500
    • Chen, C.1    Guo, P.2
  • 31
    • 0035866620 scopus 로고    scopus 로고
    • Chemical modification patterns of active and inactive as well as procapsid-bound and unbound DNA-packaging RNA of baterial virus phi29
    • Zhang, C., Trottier, M., Chen, C., and Guo, P. (2001) Chemical modification patterns of active and inactive as well as procapsid-bound and unbound DNA-packaging RNA of baterial virus phi29, Virology 281, 281-293.
    • (2001) Virology , vol.281 , pp. 281-293
    • Zhang, C.1    Trottier, M.2    Chen, C.3    Guo, P.4
  • 32
    • 0035980116 scopus 로고    scopus 로고
    • Three-dimensional interaction of phi29 pRNA dimer probed by chemical modification interference, cryo-AFM, and cross-linking
    • Mat-Arip, Y., Garver, K., Chen, C., Sheng, S., Shao, Z., and Guo, P. (2001) Three-dimensional interaction of phi29 pRNA dimer probed by chemical modification interference, cryo-AFM, and cross-linking, J. Biol. Chem. 276, 32575-32584.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32575-32584
    • Mat-Arip, Y.1    Garver, K.2    Chen, C.3    Sheng, S.4    Shao, Z.5    Guo, P.6
  • 33
    • 0033591710 scopus 로고    scopus 로고
    • Photoinduced cross-linking of RNA by cis-Rh(phen)2C12+ and cis-Rh(phen)(phi)C12+: A new family of light activatable nucleic acid cross-linking agents
    • Mohammad, T., Chen, C., Guo, P., and Morrison, H. (1999) Photoinduced cross-linking of RNA by cis-Rh(phen)2C12+ and cis-Rh(phen)(phi)C12+: a new family of light activatable nucleic acid cross-linking agents, Bioorg. Med. Chem. Lett. 9, 1703-1708.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 1703-1708
    • Mohammad, T.1    Chen, C.2    Guo, P.3    Morrison, H.4
  • 34
    • 0036761372 scopus 로고    scopus 로고
    • Inplication of the prohead RNA in phage phi29 DNA packaging
    • Bourassa, N., and Major, F. (2002) Inplication of the prohead RNA in phage phi29 DNA packaging, Biochimie 84, 945-951.
    • (2002) Biochimie , vol.84 , pp. 945-951
    • Bourassa, N.1    Major, F.2
  • 35
    • 0030893424 scopus 로고    scopus 로고
    • Use of circular permutation to assess six bulges and four loops of DNA-packaging pRNA of bacteriophage φ29
    • Zhang, C. L., Tellinghuisen, T., and Guo, P. (1997) Use of circular permutation to assess six bulges and four loops of DNA-packaging pRNA of bacteriophage φ29, RNA 3, 315-323.
    • (1997) RNA , vol.3 , pp. 315-323
    • Zhang, C.L.1    Tellinghuisen, T.2    Guo, P.3
  • 37
    • 0028351893 scopus 로고
    • Building a kinetic framework for group II intron ribozyme activity: Quantitation of interdomain binding and reaction rate
    • Pyle, A. M., and Green, J. B. (1994) Building a kinetic framework for group II intron ribozyme activity: quantitation of interdomain binding and reaction rate, Biochemistry 33, 2716-2725.
    • (1994) Biochemistry , vol.33 , pp. 2716-2725
    • Pyle, A.M.1    Green, J.B.2
  • 38
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan, J. F., and Uhlenbeck, O. C. (1989) Synthesis of small RNAs using T7 RNA polymerase, Methods Enzymol. 180, 51-62.
    • (1989) Methods Enzymol. , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 39
    • 0029410699 scopus 로고
    • Group II intron ribozymes that cleave DNA and RNA linkages with similar efficiency, and lack contacts with substrate 2′-hydroxyl groups
    • Griffin, E. A., Qin, Z., Michels, W. J., and Pyle, A. M. (1995) Group II intron ribozymes that cleave DNA and RNA linkages with similar efficiency, and lack contacts with substrate 2′-hydroxyl groups, Chem. Biol. 2, 761-770.
    • (1995) Chem. Biol. , vol.2 , pp. 761-770
    • Griffin, E.A.1    Qin, Z.2    Michels, W.J.3    Pyle, A.M.4
  • 40
    • 0024283277 scopus 로고
    • DNA and RNA sequence determination based on phosphorothioate chemistry
    • Gish, G., and Eckstein, F. (1988) DNA and RNA sequence determination based on phosphorothioate chemistry, Science 240, 1520-1522.
    • (1988) Science , vol.240 , pp. 1520-1522
    • Gish, G.1    Eckstein, F.2
  • 41
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix, R. W. (1978) Symmetry mismatch and DNA packaging in large bacteriophages, Proc. Natl. Acad. Sci. U.S.A. 75, 4779-4783.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 42
    • 0028072693 scopus 로고
    • Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer
    • Gohlke, C., Murchie, A. I., Lilley, D. M., and Clegg, R. M. (1994) Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer, Proc. Natl. Acad. Sci. U.S.A. 91, 11660-11664.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11660-11664
    • Gohlke, C.1    Murchie, A.I.2    Lilley, D.M.3    Clegg, R.M.4
  • 43
    • 0027973506 scopus 로고
    • A three-dimensional model for the hammerhead ribozyme based on fluorescence measurements
    • Tuschl, T., Gohlke, C., Jovin, T., 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.3    Westhof, E.4    Eckstein, F.5
  • 44
    • 0031800080 scopus 로고    scopus 로고
    • Global structure of four-way RNA junctions studied using fluorescence resonance energy transfer
    • Walter, F., Murchie, A. I., Duckett, D. R., and Lilley, D. M. (1998) Global structure of four-way RNA junctions studied using fluorescence resonance energy transfer, RNA 4, 719-728.
    • (1998) RNA , vol.4 , pp. 719-728
    • Walter, F.1    Murchie, A.I.2    Duckett, D.R.3    Lilley, D.M.4
  • 45
    • 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
  • 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
    • 0034711046 scopus 로고    scopus 로고
    • Helical junctions as determinants for RNA folding: Origin of tertiary structure stability of the hairpin ribozyme
    • Klostermeier, D., and Millar, D. P. (2000) Helical junctions as determinants for RNA folding: origin of tertiary structure stability of the hairpin ribozyme, Biochemistry 39, 12970-12978.
    • (2000) Biochemistry , vol.39 , pp. 12970-12978
    • Klostermeier, D.1    Millar, D.P.2
  • 48
    • 0032559410 scopus 로고    scopus 로고
    • Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA
    • Orr, J. W., Hagerman, P. J., and Williamson, J. R. (1998) Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA, J. Mol. Biol. 275, 453-464.
    • (1998) J. Mol. Biol. , vol.275 , pp. 453-464
    • Orr, J.W.1    Hagerman, P.J.2    Williamson, J.R.3
  • 49
    • 0037093486 scopus 로고    scopus 로고
    • The global structure of the VS ribozyme
    • Lafontaine, D. A., Norman, D. G., and Lilley, D. M. (2002) The global structure of the VS ribozyme, EMBO J. 21, 2461-2471.
    • (2002) EMBO J. , vol.21 , pp. 2461-2471
    • Lafontaine, D.A.1    Norman, D.G.2    Lilley, D.M.3
  • 50
    • 0032552882 scopus 로고    scopus 로고
    • Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs
    • Xia, T., SantaLucia, J. J., Burkard, M. E., Kierzek, R., Schroeder, S. J., Jiao, X., Cox, C., and Turner, D. H. (1998) Thermodynamic parameters for an expanded nearest-neighbor model for formation of RNA duplexes with Watson-Crick base pairs, Biochemistry 37, 14719-14735.
    • (1998) Biochemistry , vol.37 , pp. 14719-14735
    • Xia, T.1    Santalucia, J.J.2    Burkard, M.E.3    Kierzek, R.4    Schroeder, S.J.5    Jiao, X.6    Cox, C.7    Turner, D.H.8
  • 52
    • 0026427239 scopus 로고
    • Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups
    • Pyle, A. M., and Cech, T. R. (1991) Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups, Nature 350, 628-631.
    • (1991) Nature , vol.350 , pp. 628-631
    • Pyle, A.M.1    Cech, T.R.2
  • 53
    • 0027209722 scopus 로고
    • The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction
    • Herschlag, D., Eckstein, F., and Cech, T. R. (1993) The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction, Biochemistry 32, 8312-8321.
    • (1993) Biochemistry , vol.32 , pp. 8312-8321
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 54
    • 0027181643 scopus 로고
    • Contributions of 2′-hydroxyl groups of an RNA substrate to binding and catalysis by the Tetrahymena ribozyme. An energetic picture of an active site composed of RNA
    • Herschlag, D., Eckstein, F., and Cech, T. R. (1993) Contributions of 2′-hydroxyl groups of an RNA substrate to binding and catalysis by the Tetrahymena ribozyme. An energetic picture of an active site composed of RNA, Biochemists 32, 8299-8311.
    • (1993) Biochemists , vol.32 , pp. 8299-8311
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 55
    • 0029670279 scopus 로고    scopus 로고
    • Catalytic role of 2′-hydroxyl groups within a group II intron active site
    • Abramovitz, D. L., Friedman, R. A., and Pyle, A. M. (1996) Catalytic role of 2′-hydroxyl groups within a group II intron active site, Science 271, 1410-1413.
    • (1996) Science , vol.271 , pp. 1410-1413
    • Abramovitz, D.L.1    Friedman, R.A.2    Pyle, A.M.3
  • 56
    • 0033529336 scopus 로고    scopus 로고
    • Energetics and cooperativity of tertiary hydrogen bonds in RNA structure
    • Silverman, S. K., and Cech, T. R. (1999) Energetics and cooperativity of tertiary hydrogen bonds in RNA structure, Biochemistry 38, 8691-8702.
    • (1999) Biochemistry , vol.38 , pp. 8691-8702
    • Silverman, S.K.1    Cech, T.R.2
  • 57
    • 0037016023 scopus 로고    scopus 로고
    • Energetics of hydrogen bond networks in RNA: Hydrogen bonds surrounding G+1 and U42 are the major determinants for the tertiary structure stability of the hairpin ribozymes
    • Klostermeier, D., and Millar, D. P. (2002) Energetics of hydrogen bond networks in RNA: hydrogen bonds surrounding G+1 and U42 are the major determinants for the tertiary structure stability of the hairpin ribozymes, Biochemistry 41, 14095-14102.
    • (2002) Biochemistry , vol.41 , pp. 14095-14102
    • Klostermeier, D.1    Millar, D.P.2
  • 58
    • 0041519434 scopus 로고    scopus 로고
    • 2′-mercaptonucleotide interference reveals regions of close packing within the folded RNA molecules
    • Schwans, J. P., Cortez, C. N., Olvera, J. M., and Piccirilli, J. A. (2003) 2′-Mercaptonucleotide interference reveals regions of close packing within the folded RNA molecules, J. Am. Chem. Soc. 125, 10012-10018.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10012-10018
    • Schwans, J.P.1    Cortez, C.N.2    Olvera, J.M.3    Piccirilli, J.A.4
  • 59
    • 0027256149 scopus 로고
    • Multiple magnesium ions in the ribonuclease P reaction mechanism
    • Smith, D., and Pace, N. R. (1993) Multiple magnesium ions in the ribonuclease P reaction mechanism, Biochemistry 32, 5273-5281.
    • (1993) Biochemistry , vol.32 , pp. 5273-5281
    • Smith, D.1    Pace, N.R.2
  • 60
    • 0030929889 scopus 로고    scopus 로고
    • A magnesium ion core at the heart of a ribozyme domain
    • Cate, J. H., Hanna, R. L., and Doudna, J. A. (1997) A magnesium ion core at the heart of a ribozyme domain, Nat. Struct. Biol. 4. 553-558.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 553-558
    • Cate, J.H.1    Hanna, R.L.2    Doudna, J.A.3
  • 61
    • 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′-moeity of the guanosine nucleophile in the Tetrahymena group I ribozyme
    • Shan, S., 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′-moeity of the guanosine nucleophile in the Tetrahymena group I ribozyme, Biochemistry 38, 10958-10975.
    • (1999) Biochemistry , vol.38 , pp. 10958-10975
    • Shan, S.1    Herschlag, D.2
  • 62
    • 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
  • 63
    • 0029956116 scopus 로고    scopus 로고
    • RNA hydration: A detailed look
    • Egli, M., Portmann, S., and Usman, N. (1996) RNA hydration: a detailed look, Biochemistry 35, 8489-8494.
    • (1996) Biochemistry , vol.35 , pp. 8489-8494
    • Egli, M.1    Portmann, S.2    Usman, N.3
  • 64
    • 0035864365 scopus 로고    scopus 로고
    • An important 2′-OH group for an RNA-protein interaction
    • Hou, Y., Zhang, X., Holland, J. A., and Davis, D. R. (2001) An important 2′-OH group for an RNA-protein interaction, Nucleic-Acids Res. 29, 976-985.
    • (2001) Nucleic-Acids Res. , vol.29 , pp. 976-985
    • Hou, Y.1    Zhang, X.2    Holland, J.A.3    Davis, D.R.4
  • 65
    • 0035824877 scopus 로고    scopus 로고
    • Modifying the specificity of an RNA backbone contact
    • Dertinger, D., Dale, T., and Uhlenbeck, O. C. (2001) Modifying the specificity of an RNA backbone contact, J. Mol. Biol. 314, 649-654.
    • (2001) J. Mol. Biol. , vol.314 , pp. 649-654
    • Dertinger, D.1    Dale, T.2    Uhlenbeck, O.C.3
  • 66
    • 2942577733 scopus 로고    scopus 로고
    • Application of NMR and EPR methods to the study of RNA, Curr
    • Qin, P. Z., and Dieckmann, T. (2004) Application of NMR and EPR methods to the study of RNA, Curr. Opin. Struct. Biol. 14, 350-359.
    • (2004) Opin. Struct. Biol. , vol.14 , pp. 350-359
    • Qin, P.Z.1    Dieckmann, T.2
  • 67
    • 14244273876 scopus 로고    scopus 로고
    • In the fluorescent spotlight: Global and local conformational changes of small catalytic RNAs
    • Walter, N. G., Harris, D. A., Pereira, M. J., and Rueda, D. (2002) In the fluorescent spotlight: global and local conformational changes of small catalytic RNAs, Biopolymers 61, 224-242.
    • (2002) Biopolymers , vol.61 , pp. 224-242
    • Walter, N.G.1    Harris, D.A.2    Pereira, M.J.3    Rueda, D.4
  • 68
    • 0035849534 scopus 로고    scopus 로고
    • Quantitative analysis of the GAAA tetraloop/receptor interaction in solution: A site-directed spin labeling study
    • Qin, P. Z., Butcher, S. E., Feigon, J., and Hubbell, W. L. (2001) Quantitative analysis of the GAAA tetraloop/receptor interaction in solution: a site-directed spin labeling study, Biochemistry 40, 6929-6936.
    • (2001) Biochemistry , vol.40 , pp. 6929-6936
    • Qin, P.Z.1    Butcher, S.E.2    Feigon, J.3    Hubbell, W.L.4
  • 69
    • 0035925208 scopus 로고    scopus 로고
    • Site-specific incorporation of nitroxide spin-labels into internal sites of the TAR RNA. Structure-dependent dynamics of RNA by EPR spectroscopy
    • Edwards, T. E., Okonogi, T. M., Robinson, B. H., and Sigurdsson, S. T. (2001) Site-specific incorporation of nitroxide spin-labels into internal sites of the TAR RNA. Structure-dependent dynamics of RNA by EPR spectroscopy, J. Am. Chem. Soc. 123, 1527-1528.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1527-1528
    • Edwards, T.E.1    Okonogi, T.M.2    Robinson, B.H.3    Sigurdsson, S.T.4
  • 70
    • 0037984764 scopus 로고    scopus 로고
    • Monitoring RNA base structure and dynamics using site-directed spin labeling
    • Qin, P. Z., Hideg, K., Feigon, J., and Hubbell, W. L. (2003) Monitoring RNA base structure and dynamics using site-directed spin labeling, Biochemistry 42, 6772-6783.
    • (2003) Biochemistry , vol.42 , pp. 6772-6783
    • Qin, P.Z.1    Hideg, K.2    Feigon, J.3    Hubbell, W.L.4


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